VOLUME THREE HUNDRED AND TWENTY TWO INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY International Review of Cell and Molecular Biology Series Editors GEOFFREY H BOURNE JAMES F DANIELLI KWANG W JEON MARTIN FRIEDLANDER JONATHAN JARVIK 1949—1988 1949—1984 1967— 1984—1992 1993—1995 Editorial Advisory Board PETER L BEECH ROBERT A BLOODGOOD BARRY D BRUCE DAVID M BRYANT KEITH BURRIDGE HIROO FUKUDA MAY GRIFFITH KEITH LATHAM WALLACE F MARSHALL BRUCE D MCKEE MICHAEL MELKONIAN KEITH E MOSTOV ANDREAS OKSCHE MADDY PARSONS TERUO SHIMMEN ALEXEY TOMILIN GARY M WESSEL VOLUME THREE HUNDRED AND TWENTY TWO INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY Edited by KWANG W JEON Department of Biochemistry University of Tennessee Knoxville, Tennessee AMSTERDAM • BOSTON • HEIDELBERG • LONDON NEW YORK • OXFORD • PARIS • SAN DIEGO SAN FRANCISCO • SINGAPORE • SYDNEY • TOKYO Academic Press is an imprint of Elsevier Academic Press is an imprint of Elsevier 50 Hampshire Street, 5th Floor, Cambridge, MA 02139, USA 525 B Street, Suite 1800, San Diego, CA 92101-4495, USA 125 London Wall, London EC2Y 5AS, UK The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, UK Copyright © 2016 Elsevier Inc All rights reserved No part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or any information storage and retrieval system, without permission in writing from the publisher Details on how to seek permission, further information about the Publisher’s permissions policies and our arrangements with organizations such as the Copyright Clearance Center and the Copyright Licensing Agency, can be found at our website: www.elsevier.com/permissions This book and the individual contributions contained in it are protected under copyright by the Publisher (other than as may be noted herein) Notices Knowledge and best practice in this field are constantly changing As new research and experience broaden our understanding, changes in research methods, professional practices, or medical treatment may become necessary Practitioners and researchers must always rely on their own experience and knowledge in evaluating and using any information, methods, compounds, or experiments described herein In using such information or methods they should be mindful of their own safety and the safety of others, including parties for whom they have a professional responsibility To the fullest extent of the law, neither the Publisher nor the authors, contributors, or editors, assume any liability for any injury and/or damage to persons or property as a matter of products liability, negligence or otherwise, or from any use or operation of any methods, products, instructions, or ideas contained in the material herein ISBN: 978-0-12-804809-2 ISSN: 1937-6448 For information on all Academic Press publications visit our website at http://store.elsevier.com/ CONTRIBUTORS Fiorenza Accordi Department of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, Italy Jaap D van Buul Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Claudio Chimenti Department of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, Italy Annalena Civinini Department of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, Italy Enrico Crivellato Department of Experimental and Clinical Medicine, Section of Anatomy, University of Udine, Italy Anna E Daniel Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Lisa J Edens Department of Molecular Biology, University of Wyoming, Laramie, WY, United States of America Valentina P Gallo Department of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, Italy Stephanie L Gupton Department of Cell Biology and Physiology, University of North Carolina, Chapel Hill, NC, United States of America; Neuroscience Center and Curriculum in Neurobiology, University of North Carolina, Chapel Hill, NC, United States of America; Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, United States of America Predrag Jevtic´ Department of Molecular Biology, University of Wyoming, Laramie, WY, United States of America ix x Contributors Eric J Kremer Institut de Ge´ne´tique Mole´culaire de Montpellier, Universite´ de Montpellier, Montpellier, France Jeffrey Kroon Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Daniel L Levy Department of Molecular Biology, University of Wyoming, Laramie, WY, United States of America Fabien Loustalot Institut de Ge´ne´tique Mole´culaire de Montpellier, Universite´ de Montpellier, Montpellier, France Shalini Menon Department of Cell Biology and Physiology, University of North Carolina, Chapel Hill, NC, United States of America Francisco Rivero Hull York Medical School, University of Hull, Hull, United Kingdom Sara Salinas Institut de Ge´ne´tique Mole´culaire de Montpellier, Universite´ de Montpellier, Montpellier, France Ilse Timmerman Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Lidija D Vukovic´ Department of Molecular Biology, University of Wyoming, Laramie, WY, United States of America Cortney Chelise Winkle Neuroscience Center and Curriculum in Neurobiology, University of North Carolina, Chapel Hill, NC, United States of America Huajiang Xiong Hull York Medical School, University of Hull, Hull, United Kingdom CHAPTER ONE New Insights into Mechanisms and Functions of Nuclear Size Regulation Lidija D Vuković, Predrag Jevtić, Lisa J Edens, Daniel L Levy* Department of Molecular Biology, University of Wyoming, [18_TD$IF]Laramie, WY, United States of America *Corresponding author E-mail: dlevy1@uwyo.edu Contents Introduction Overview of Cellular Structures and Activities that Contribute to Nuclear Size Determination 2.1 Nuclear Structure and Models of Organelle Size Control 2.2 Genome Size and Ploidy 2.3 Chromatin State 2.4 Cell Size and Nucleocytoplasmic Ratio 2.5 Nucleocytoplasmic Transport 2.6 Intranuclear Structures 2.7 Extranuclear Structures 2.8 Cell-Cycle Effects 2.9 Signaling Pathways Model Systems to Elucidate Mechanisms of Nuclear Size Regulation 3.1 Tetrahymena thermophila 3.2 Yeasts and Fungi 3.3 Plants 3.4 Caenorhabditis elegans 3.5 Drosophila melanogaster 3.6 Zebrafish 3.7 Xenopus 3.8 Mammalian Model Systems Functional Significance of Nuclear Size and Morphology 4.1 Chromosome Positioning, Chromatin Organization, and Gene Expression 4.2 Nuclear Mechanics and Cell Migration 4.3 Nuclear Size and Morphology Changes in Cancer 4.4 Nuclear Envelopathies International Review of Cell and Molecular Biology, Volume 322 ISSN 1937-6448 http://dx.doi.org/10.1016/bs.ircmb.2015.11.001 © 2016 Elsevier Inc All rights reserved 3 10 11 12 13 15 18 18 20 21 22 24 26 26 31 33 33 35 36 39 Lidija D Vuković et al Conclusions Acknowledgments References 40 41 42 Abstract Nuclear size is generally maintained within a defined range in a given cell type Changes in cell size that occur during cell growth, development, and differentiation are accompanied by dynamic nuclear size adjustments in order to establish appropriate nuclear-to-cytoplasmic volume relationships It has long been recognized that aberrations in nuclear size are associated with certain disease states, most notably cancer Nuclear size and morphology must impact nuclear and cellular functions Understanding these functional implications requires an understanding of the mechanisms that control nuclear size In this review, we first provide a general overview of the diverse cellular structures and activities that contribute to nuclear size control, including structural components of the nucleus, effects of DNA amount and chromatin compaction, signaling[20_TD$IF] and transport pathways that impinge on the nucleus, extranuclear structures, and cell cycle state We then detail some of the key mechanistic findings about nuclear size regulation that have been gleaned from a variety of model organisms Lastly, we review studies that have implicated nuclear size in the regulation of cell and nuclear function and speculate on the potential functional significance of nuclear size in chromatin organization, gene expression, nuclear mechanics, and disease With many fundamental cell biological questions remaining to be answered, the field of nuclear size regulation is still wide open INTRODUCTION Cell and nuclear sizes differ greatly among different species, as well as within the same organism when comparing different cell types Even in the same tissue, cell and nuclear sizes can vary depending on the developmental stage, state of cell differentiation, a variety of external factors, and cellular transformation How nuclear size and shape affect cell physiology is still unclear, but it is certainly possible that nuclear morphology impacts chromatin organization and gene expression Elucidating the functional significance of nuclear size necessitates an understanding of the mechanisms that control nuclear size This is particularly important in the case of pathologies in which nuclear morphology is altered, most notably cancer, where it is unclear if changes in nuclear size and shape are a cause or consequence of disease In this review, we first provide a general overview of the diverse cellular structures and activities that are relevant to the regulation of nuclear size, New Insights into Mechanisms and Functions of Nuclear Size Regulation including ploidy, chromatin condensation, the nucleocytoplasmic ratio, and nuclear transport (Fig[21_TD$IF] 1) We next turn to different model systems that have and will continue to shed light on mechanisms of nuclear size regulation (Fig[21_TD$IF] 2) We review how nuclear size is regulated by soluble transport factors, structural components of the nuclear envelope [2_TD$IF](NE), signaling pathways, and extranuclear structures like the endoplasmic reticulum and cytoskeleton Lastly, we discuss demonstrated or proposed roles for nuclear size in chromosome organization, gene expression, nuclear mechanics, and pathology In the last decade, the great complexity of nuclear structure and function has begun to emerge, and here we provide a broad overview of how the regulation of nuclear morphology contributes to this complexity OVERVIEW OF CELLULAR STRUCTURES AND ACTIVITIES THAT CONTRIBUTE TO NUCLEAR SIZE DETERMINATION Organelle size and morphology must have important implications for organelle and cellular function (Edens et al., 2013; Heald and Cohen-Fix, 2014; Jevtic et al., 2014) Understanding these functional implications first requires elucidation of the mechanisms that control organelle size When it comes to nuclear size regulation, a number of potential mechanisms have been implicated including structural components of the nucleus, effects of DNA amount and chromatin compaction, signaling and transport pathways that impinge on the nucleus, extranuclear structures, and cell cycle state In this section, we provide a general overview of these diverse mechanisms that contribute to nuclear size control Each subsection deals with a general theme relevant to the regulation of nuclear size At the end of each subsection, we refer to later sections in the review that delve into greater detail with respect to that mechanism 2.1 Nuclear [23_TD$IF]Structure and Models of Organelle Size Control The NE is composed of a double lipid bilayer The outer nuclear membrane (ONM) is a continuous extension of the endoplasmic reticulum (ER) In metazoan nuclei, the inner nuclear membrane (INM) is lined on its nucleoplasmic face by the nuclear lamina, a meshwork of intermediate lamin filaments The INM and ONM are fused at sites of nuclear pore complex (NPC) insertion The NPC mediates nucleocytoplasmic transport of proteins and mRNA [24_TD$IF]Linker of nucleoskeleton and cytoskeleton (LINC) [(Figure_1)TD$IG] Lidija D Vuković et al 394 Valentina P Gallo et al Vallejo, D., Habib, M.R., Delgado, N., Vaasjo, L.O., Croll, R.P., Miller, M.W., 2014 Localization of tyrosine hydroxylase-like immunoreactivity in the nervous systems of Biomphalaria glabrata and Biomphalaria alexandrina, intermediate hosts for schistosomiasis J Comp Neurol 522, 2532–2552 Van Marle, J., 1977 Contribution to the knowledge of the nervous system in the tentacles of some Coelenterates Bijdr Dierkd 46, 219–260 Vanderlinden, C., Mallefet, J., 2004 Synergic effects of tryptamine and octopamine on Ophiuroid luminescence (Echinodermata) J Exp Biol 207, 3749–3756 Venturini, G., Silei, O., Palladini, A., Margotta, V., 1984 Aminergic neurotransmitters and adenylate cyclase in Hydra Comp Biochem Physiol C78, 345–348 Westfall, J.A., Elliott, S.R., MohanKumar, P.S., Carlin, R.W., 2000 Immunocytochemical evidence for biogenic amines and immunogold labeling of serotonergic synapses in tentacles of Aiptasia pallida (Cnidaria, Anthozoa) Invert Biol 119, 370–378 Wood, J.G., Lentz, T.L., 1964 Histochemical localization of amines in Hydra and in the sea anemones Nature 201, 88–90 Yamamoto, S., Seto, E.S., 2014 Dopamine dynamics and signaling in Drosophila: an overview of genes, drugs and behavioral paradigms Exp Anim 63, 107–119 Zaccone, G., Abelli, L., Saltapietro, L., Zaccone, D., Macrı`, B., Marino, F., 2011a Nervous control of photophores in luminescent fishes Acta Histochem 113, 387–394 Zaccone, G., Abelli, L., Saltapietro, L., Zaccone, D., Manganaro, M., Marino, F., 2011b Immunolocalization of neurotransmitter-synthesizing enzymes and neuropeptides with associated receptors in the photophores of the hatchetfish, Argyropelecus hemigymnus Cocco, 1829 Acta Histochem 113, 457–464 Zaitseva, O.V., Markosova, T.G., Smirnov, R.V., 2007 Monoamine- and peptide-containing elements in the body wall and nervous trunks of Nemerteans Russ J Mar Biol 33, 245–253 Zega, G., Pennati, R., Groppelli, S., Sotgia, C., De Bernardi, F., 2005 Dopamine and serotonin modulate the onset of metamorphosis in the Ascidian Phallusia mammillata Dev Biol 282, 246–256 Zhang, H., Zhou, Z., Yue, F., Wang, L., Yang, C., Wang, M., Song, L., 2014 The modulation of catecholamines on immune response of scallop Chlamys farreri under heat stress Gen Comp Endocrinol 195, 116–124 Zhou, Z., Wang, L., Yang, J., Zhang, H., Kong, P., Wang, M., Qiu, L., Song, L., 2011a A dopamine beta hydroxylase from Chlamysfarreri and its induced mRNA expression in the haemocytes after LPS stimulation Fish Shellfish Immun 30, 154–162 Zhou, Z., Wang, L., Shi, X., Zhang, H., Gao, Y., Wang, M., Kong, P., Qiu, L., Song, L., 2011b The modulation of catecholamines to the immune response against bacteriaVibrio anguillarum challenge in scallop Chlamys farreri Fish Shellfish Immun 31, 1065–1071 INDEX A AAA+ ATPases, 30 abLIM See Actin-binding LIM (abLIM) protein Ace2 activates transcription, 21 Acidic phospholipids, 133 Actin-adapter proteins ezrin/radixin/moesin (ERM) family, 282 Actin-binding LIM (abLIM) protein, 201 Actin-binding proteins, 150, 187 actin-bundling proteins, 195 actin-monomer binding proteins, 195 actin-nucleating proteins, 187 barbed-end binding proteins, 192 cortexillin I, 139 F-actin motor proteins, 201 F-actin-severing proteins, 197 membrane-actin linker proteins, 202 other F-actin-binding proteins, 199 Actin-bundling proteins, 195 CRP1, 196 fascin, 195 palladin, 196 Actin cytoskeleton remodeling, 61 Actin-dependent protrusion, 158 Actin-monomer binding proteins, 195 profilin, 195 Actin/MT-linking actin-binding proteins, 222 drebrin, 222 IQGAP1, 224 Pod1, 223 TcTex-1, 223 Actin-nucleating proteins, 187 Arp2/3 and nucleation promoting factors, 187 Cordon-Bleu (Cobl), 190 formins, 191 diaphanous, 191 Actin polymerization, 150 Adaptor protein (AP-2) complex, 304 Adenomatous polyposis coli (APC), 214 Adherens junctions (AJs), 297 cell–cell contacts, 298 Adherent leukocytes, 294 Adhesion receptor, 287 Adrenaline low salinity effects, 369 metabolic pathways of, 360 AdV fiber knob (FK), 336 Amphibian eggs, 26 Amphipholis squamata, 374 Amphiura ¢liformis, 374 Aneuploidy, 37 Animal nuclei, 21 Antibodies, leukocytes crossing, 286 Anti-PECAM-1 antibodycoated magnetic beads, 308 Antisense oligonucleotides, 208 APC See Adenomatous polyposis coli (APC) Apoptosis, 61, 123, 131 Apostichopus japonicas, 374 Arabidopsis thaliana myosin XI, 13 Arf6-dependent pathway, 348 Aromatic L-amino acid decarboxylase, 361 Ascidian Ciona intestinalis neural crest-likecells(NCLC), 375 Ashbya gossypii, 21 Asteroidea, 374 Atrioventricular-node cell–cell junctions, 345 Axon, 182, 185, 186, 191, 196, 203, 207, 214, 221 B Bacterial lipopolysaccharide, 368 Barbed-end binding proteins, 192 Ena/VASP protein family, 192 lamellipodin, 194 395 396 Barnacle Megabalanus rosa planktonic larva cypris, 378 Basolateral membrane protein targeting, 332 BigMic, overexpression of, 18 Bioluminescence, 362, 363 Blood-brain barrier, 298 Bolenopsis infundibulum, 364 BoNTA See Botulinum neurotoxin A (BoNTA) BoNTC1 See Botulinum neurotoxin C (BoNTC1) Botulinum neurotoxin A (BoNTA), 253 Botulinum neurotoxin C (BoNTC1), 255 Bradykinin, 302, 304 Brain CAR signaling, 346 endothelia, 295 Brambleberry (bmb), 26 Branchiostoma lanceolatum, 375 BRCA tumor suppressor, 38 Broad actin-rich protrusions, 150 C N-Cadherin, 300 Cadherin–catenin complex, 302 Caenorhabditis elegans, 36, 62, 372 embryos, 22 CALI See Chromophore-assisted laser inactivation (CALI) cAMP, 117, 118, 121, 143, 156, 160 Cancer-associated disruptions, 38 Cancer cells CAR signaling, 349 characteristics of, 36 MAPK pathway, 349 Cancer nuclei, 37 Cancer treatment, 39 Capping protein (CP), 219 Cardiomyopathy, 39 Catecholamines (CA), 359 biogenic amines, 359 biosynthetic enzymes TH, immunostaining of, 366 -containing neurons, 368 -induced fluorescence, 374 synthesis, 366 taxon of, 362 Index α-Catenin covalent fusion of, 301 CAV-2, in brain structures, 335 CCL5 (RANTES) genes, 347 CD99/CD99L2, functional blocking of, 300 CD44-E-selectin interaction, 284 Cdk activity, 14 CD99-like (CD99L2), 300 CD68+ macrophages, 296 CD8+T cells, 285 CEDNIK See Cerebral dysgenesis, neuropathy, ichthyosis, and keratoderma (CEDNIK) syndrome Cell communication, 359 Cell computed tomographic imaging, 39 Cell cortex, 150 Cell cycle regulation, 123 Cell division cycle associated (CDCA2), 34 Cell engulfment, 37 Cell morphology, 118 Cell motility, 118 Cell polarity, 156 Central nervous system, 366 Cerebral dysgenesis, neuropathy, ichthyosis, and keratoderma (CEDNIK) syndrome, 254 Chaetopterus variopedatus, 368 Chelicerata, 371 Chemotaxis, 118, 156 Rho signaling, 157 Chlamys farreri, 369 Chlamys farreri, 366 Cholera toxin B (CTxB), 342 Chromaffin-like cells, 366 Chromaffin stain, 366 Chromatin-bound Dppa2, 14 Chromatin condensation, Chromatin decondensation, 34 Chromophore-assisted laser inactivation (CALI), 208 Chromosomal translocations, 38 Chromosome positioning, 33 Chromosome structure, 15 Ciliary activity, 366 Ciona intestinalis embryos, 380 Index Ciona savignyi, 380 Clathrin-coated vesicle (CCV) machinery, 337 CLIP See Cytoplasmic linker protein (CLIP) CNEP-1Δ embryos transmission electron microscopy, 23 Cnidarian hydrozoan, 377 Collapsin response mediator proteins (CRMP), 210 Colorectal cancer, 38 Complement receptor-3 (CR-3), 285 Confocal microscopy, 296 Control nuclear size model organisms and factors, Conventional protein kinase C (cPKC) 15, 28 Coronin, 161 Coronin A, 135 Corticotropin-releasing factor (CRF), 366 Coxsackievirus and adenovirus receptor (CAR), 327 CAM ECD shedding, 346 clathrin-adaptor protein (AP), 328 colocalization of, 342 CVB-induced myocarditis, 349 E-cadherin level, 344 endocytosis, 336 viral-mediated, 340 endogenous murine, 339 epithelial γδ T cells, 348 FKCAV degradation, 342 gene expression, 333 at axon terminal, 341 in cells/tissues, 330 localization in neurons ex vivo, 339 regulation of, 331 homo- and heterophilic interactions, 346 ICD phosphorylation by PKC and Src triggers, 333 interactome, 343 KO mice, 345 localization in lipid rafts, 336 membrane dynamics, 332, 337 endocytosis, 336–342 targeting to plasma membrane, 332–336 397 nephrotic foot processes, 345 overexpression in rat hippocampal neurons, 335 overview of, 327 participates to cardiomyocyte homeostasis, 345 protein, 327 posttranslational modifications, 328 protein–protein interactions, 344 retinoblastoma protein (pRb), 349 γ-secretase complex, 346 signaling, 345 brain, 346 cancer cells, 349 epithelial cells, 344–345 heart, 345 immunity, 348 protein trafficking, role, 343 viral infection, 347–348 and splice variants, 327 transmembrane (TM) domain, 328 Coxsackievirus B type (CVB3), 348 Coxsackieviruses (CVB), 327 CP See Capping protein (CP) cPKC activator, 17 Crassostrea gigas, 366, 378 Crassostrea iridalei, 378 Crithidia fasciculata, 361 CRMP See Collapsin response mediator proteins (CRMP) Crustacea, 371 C-terminal CaaX motif, 29 C-type lectin domain, 284 CXADR expression, 331 Cxadr gene, 327 human and mouse, 328 promoter, 332 region, 331 CXC chemokine receptor (CXCR2), 304 CXCL8 (IL-8) genes, 347 CXCL10 (IP-10) genes, 347 Cyclin-dependent kinases (Cdks), 13 Cytokine, 37, 125, 130, 166, 191, 260, 280, 284, 304, 331, 333, 349 Cytokinesis, 118, 260 Cytoplasmic dynein motor complex, 223 398 Cytoplasmic linker protein (CLIP), 212 Cytoskeletal, 182 -associated proteins, 186 in neuronal development depolymerization, 182 dynamics, 182 organization, 182 polymerization, 182 Cytoskeleton, actin-binding adapter proteins, 293 D DAF (decay-accelerating factor), 348 Darlin, 144 DCX See Doublecortin (DCX) Dendrite, 186 Dendritic markers, 183 Dendritic plasticity, 186 Density-enhanced phosphatase-1 (DEP-1), 303 Dephosphorylation, 159 Desmoglein-2, 336 Developmentally regulated brain protein (Drebrin), 222 Developmental pluripotency-associated (Dppa2) protein, 30 Dictyostelium discoideum, 62 asexual development in, 62 model organism, advantages as, 62 Rac proteins, 113 Rho GTPases, 65 effectors, 124 features/expression of, 65 functional studies of, 115 effects on actin cytoskeleton, 116 Rac1, 117 RacA, RhoBTB Protein, 123 RacB, 118 RacC, 119 RacE, 120 RacF, 121 RacG, 122 RacH, 122 guanine nucleotide exchange factors, 144 processes regulated by, 156 Index specific guanine nucleotide dissociation inhibitors (RhoGDIs), 142, 143 subcellular localization, 114 Rho signaling in, 62 cytokinesis, role in, 165 at leading front, 158 proteins involved, their occurrence in other phyla, 63 at rear, 160 role in chemotaxis toward cAMP, 156 during transit, exocytosis, 163 vesicle trafficking, 161 sexual developmental cycle in, 62 starvation, effects of, 62 Dilated cardiomyopathy (DCM), 39 Dilocarcinus pagei, 371 Dinoflagellate Gonyaulax, circadian rhythms, 363 DNA repair, 38 DNA-to-cytoplasm ratio, 27 Dopamine level of, 379 metabolic pathways of, 360 Dopamine-β-hydroxylase(DβH), 360 Dorsal root ganglion neurons (DRGs), 251 Doublecortin (DCX), 209 Drebrin, 222 Drebrin See Developmentally regulated brain protein (Drebrin) DRGs See Dorsal root ganglion neurons (DRGs) Drosophila melanogaster, 8, 24, 62 Dunnigan-type familial partial lipodystrophy (FPLD), 39 E Earthworms, 368 E-cadherin downregulation, 333 Ecdysozoa, 361 Ecteinascidia turbinata, 375 Effectors, 124, 141 Coronin A, 135 F-BAR family, 141 filamin, 138 formins, 136 399 Index ForC, 137 ForF, 137 ForH, 138 IQGAP-related proteins, 138 in cell division, 139 chemotaxis, role in, 140 development, role in, 140 P21-activated kinases, 131 WASP family proteins, 125 scar complex, 128 WASP-B, 128 Eisenia fetida, 368 Eledone cirrhosa, 366 Elmo A, 150 Elmo E, 151 Embryonic cell divisions, 22 Emery–Dreifuss muscular dystrophy (EDMD), 39 Endocytosis, 118, 260 clathrin-independent mechanisms, 260 clathrin-mediated, 260 neuritogenesis, 261 neuronal differentiation, 261 neuronal endosomes, compartmentalization of, 264 neuronal pathways of, 262 pharmacological inhibition of, 261 receptor endocytosis in neurite outgrowth, 261 spatial specificity, 263 Endogenous catecholamines, 364 Endolysosomes, 131 Endoplasmic reticulum (ER), 2, 3, 12, 265 ER-tubule shaping protein Rtn4 exhibit, Endoplasmic reticulum associated protein degradation (ERAD), 337 Endothelial cell–cell contacts, 297 Endothelial cell-cell junctions, 290 Endothelial cells, 282 from lymphatic system, 330 Endothelial membrane, 297 Endothelial PECAM-1, 300 Endothelial signaling pathways Rho-GTPases regulating leukocyte extravasation, 292 Endothelium-specific claudin-5, 298 Endothelium-specific VE-cadherin, 300 Entamoeba histolytica, 143, 361 Entamoeba trophozoites, 361 Enzyme immunoassays, 366 Epinephrine, 373, 379 Epithelial cells CAR signaling, 344–345 Equilibrium balance models, 17 ER See Endoplasmic reticulum (ER) ERM See Ezrin, radixin, and moesin (ERM) protein family ESCRT machinery, 14 E-selectin, 282 E-selectin-PSGL-1 interaction, 283 Euglenozoa, 361 Exocytic fusion, 260 Exocytosis, 248, 332 exocytic SNARE proteins, 248 vesicle tethering proteins, 258 Experimental autoimmune encephalomyelitis (EAE), 286 Extracellular matrix glycosaminoglycan hyaluronan, 284 Ezrin/radixin/moesin (ERM) family of actin-adapter proteins, 282 protein, 203 F F-actin, 118, 182 -binding proteins, 199 bundling proteins α-actinin-1, 294 tropomodulin (Tmod), 199 tropomyosins (Tm), 199 UNC-115/abLIM proteins, 200 cross-linker proteins, 294 depolymerization, 32 motor proteins, 201 myosin II, 201 polymerization, 155, 294, 296 -severing proteins, 197 ADF/Cofilin, 197 stress fibers, 289 Falck fluorescence method, 364 Falck-Hillarp methods, 362 fluorescence, 362 Fallopian tubes epithelium of, 282 400 Farnesyltransferase inhibitors, 40 Feeding, 366 Fibroblast growth factor (FGF), 302 Fibroblasts, 254 Filamin, 139 Fission yeast, FKCAV-mediated CAR endocytosis, 340 Fluorescence histochemistry, 366 Fluorescence resonance energy transfer (FRET), 115 Folic acid, 117 Formaldehyde-induced fluorescence, 360 Formins, 136 multidomain regulators of actin dynamics, 136 RasGEFL, 136 RasGEFV, 136 G GacQ protein, 154 G-actin See Globular actin (G-actin) Gain-of-function mutants, 115 Gastropod, 366 GDIs See Guanine nucleotide-dissociation inhibitors (GDIs) GEFs See Guanine nucleotide exchange factors (GEFs) Gene expression, 38 Gene fusions, 37 Globular actin (G-actin), 182 Glutathione transferase (GST), 114 Glyoxylic acid, 364 Golgi complex, 265 outposts, 265 trans-Golgi network (TGN), 332 Golgi vesicles, 265 Gonyaulax polyedra, 361, 363 Gp210 depletion, 23 G-protein-coupled receptors, 156 Green fluorescence, 366 Green fluorescent protein (GFP) technology, 114 GTPase, 267 activation, 289 Arf6, 348 functions, 267 Index neuronal, 267 Rap1, 285 GTPase activating proteins (GAPs) 61, 151, 289 Dd5P4, 152 MEGAPs, 153 other, 154 proteins with domains, 155 GTP hydrolysis, 30 Guanine exchange factor (GEF), 304 Guanine nucleotide-dissociation inhibitors (GDIs), 61, 291 Guanine nucleotide exchange factors (GEFs), 61, 144, 289, 291 conventional RhoGEFs, 145 GxcC, 146 GxcDD, 147 GxcT, 147 Myosin M, 145 other, 148 RacGEF1, 146 Roco family, 148 CZH family of Elmo, 149 CZH family of RhoGEFs, 149 Dock, 150 Elmo, 150 Zizimin, 150 proteins with domains, 155 H HaCaT cells, 32 HAdV-C5 vector transduction, 336 HAdV type (HAdV-C2), 336 Haliotis tuberculata, 366 Halocordyle disticha, 377 Harmothoe imbricata A, 368 HeLa cells, 17, 31, 34, 266 Hemicentrotus pulcherrimus, 378 Heterochromatin, distribution of, 34 Heterotrimeric G proteins, 158 Hexapoda, 371 High performance liquid chromatography with electrochemical detection (HPLC-ECD), 372 Hippocampal neurons, 223 Hirudo medicinalis, 368 401 Index Histone acetyltransferase/deacetylase (HAT/HDAC), 331 Histone deacetylase 3, 34 Histone H2A, Histone methyltransferases/demethylases (HMT/HDM), 331 Holothuria glaberrima, 376 Holothuroidea, catecholaminergic plexus, 375 Homophilic interaction, 299 HPLC methods, 361, 362, 364 HT1080 fibrosarcoma cells, Human adenovirus (HAdVs), 327 Human lung epithelial cells, 347 Human promyelocytic leukemia (HL-60) cells, 32 Human umbilical vein endothelial cells (HUVECs), 281 Hutchinson–Gilford progeria syndrome (HGPS), 39 Hydra, 362 I ICAM-1 clustering, 289, 295 Rac1 downstream, 297 ICAM-1 function, 291 ICAM-1-induced RhoA activation, 289 ICAM-1 interactions with adapter proteins, 295 ICAM-1 rings, 296 ICAM-1/VCAM-1 clustering, 293 IL-8-induced Rac1 activation, 304 Immunity, 366 CAR signaling, 348 Immunoglobulin (Ig), 288, 327 Ig-like domains, 288 Ig-variable (V-Ig) domain, 328 Immunohistochemical (antityrosinehydroxylase immunoreactivity) methods, 374 Importin-independent pathways, 11 Importins nucleocytoplasmic distribution, 11 INM protein Sun1, 40 Inositol polyphosphate 5-phosphatases, 152 Integrin LFA-1, 285 Interleukin-lβ (IL-1β), 287 Intermediate filament proteins, 182 Internalization, 284 Intracellular/interorganismal signaling molecules, 361 Invertebrates catecholaminergic system cnidaria, 362–364 ctenophora, 362–364 deuterostomia, 374 catecholamines during development/ metamorphosis, 377–380 chordata, 375 echinodermata, 374 dopamine/noradrenaline/adrenaline/ octopamine, metabolic pathways of, 360 overview of, 359 porifera, 362 protostomia, 364 annelids, 368 arthropoda, 371–372 mollusca, 366–368 nematoda, 372 nemertea, 366 platyhelminthes, 364 “protozoa” protists, 361 IQ domain-containing GTPase-activating protein (IQGAP1), 224 See IQ domain-containing GTPaseactivating protein (IQGAP1) J JAM-like (JAML), 299 K KASH domain, 32 Kugelkern (Kuk) INM protein, 25 L Lamin A, 38 Lamina-associated domains (LADs), Lamin B3 (LB3), 27 Lamin B depletion, 36 Lamin B receptor (LBR), 32 Lamin intermediate filament proteins, 29 L1-CAM substrate, 251 Leeches, 368 402 Lethal giant larvae (LGL) family, 258 Leukocytes, 304 adhesion, 289 circulating, 281 counterparts L-selectin (CD62L), 280 crawl, on endothelial cells, 285 crossing See Leukocytes crossing extravasation, 280, 306 TEM, 291, 294, 295 Leukocytes adhesion deficiency (LAD), 285 Leukocytes crossing actin adapter proteins, 293, 295 actin cytoskeleton, 293 α-actinin-1/4, 294 cortactin, 294 endothelial cell-cell junction regulation, 290, 297 adherens junctions, regulation of, 302 CD99, 299–300 PECAM-1, 299–300 serine phosphorylation, 304 tight junctions, 298–299 tyrosine phosphatases, 303 tyrosine phosphorylation, 302 VE-cadherin, 300–302 internalization, 304 shedding, 305–306 endothelial docking structure, 296 endothelial membrane protrusions, 297 endothelial stiffness, 295 ERM proteins, 293 filamin A/B F-actin cross-linker proteins, 294 hemodynamic shear forces, during leukocyte TEM, 306 mechanotransduction complex, 308 sensing shear flow, 308 shear flow as prerequisite, 307 leukocyte TEM, multistep paradigm of, 280 overview, 280 recruitment of, 280 Rho-GTPase activation cycle, 291 Rho-GTPases regulating leukocyte endothelial signaling pathways, 292 rolling/adhesion, 281–286 CD44, 284 Index E-selectin, 287 firm adhesion, 285 ICAM-1 engagement, 288 ICAM-1 expression, 288 ICAM-1 recruitment, 291 LFA-1, 285 Mac-1, 285 VCAM-1 engagement, 288 VCAM-1 expression, 288 VCAM-1 recruitment, 291 VLA-4, 286 L-Selectin, 284 P-selectin, 286 PSGL-1, 282 LGL See Lethal giant larvae (LGL) family β-Like adrenergic receptors, 362 LINE1 DNA hypomethylation, 34 Linker of nucleoskeleton and cytoskeleton (LINC) complexes, proteins, 32 Lipid rafts, 332 dependent pathway, 348 Lipin homologue, 23 NE-localized activator of, 23 Lipodystrophy, 39 Lipopolysaccharide (LPS), 287 Litopenaeus vannamei, 371 whiteleg shrimp, 373 LMNA/C gene, 39 LMNB1/LMNB2 genes, 31 Locomotion, 366 Lophotrochozoa, 361 Low-affinity interactions, 280 L-selectin, 282, 284 -deficient animals, 284 Lumbricus polyphemus, 368 Lumbricus terrestris, 368 Lung cancer cells (p16INK4A), 34 Lytechinus pictus, 378 M MacNup98A, 18 MacNup98B, 18 Macrobdella decora, 368 Macrophage-1 antigen, 283 403 Index Macropinosomes, 117 Mammalian hypothalamic-pituitaryadrenal axis, 366 MAPs See MT-associated proteins (MAPs) Marine invertebrates, 377 MBT embryos, 28 N/C volume ratio, 29 mCAR expression, in brain, 330 Megabalanus rosa, 378 Membrane-actin linker proteins, 202 Af-6/Afadin, 204 ankyrin, 203 ERM proteins, 203 Shootin1, 204 spectrin, 202 Membrane-associated proteins, 342 Membrane proteins, 248 Membrane trafficking, 246 Metamorphosis, 377 Methyl-CpG-binding protein (MeCP2), 32 MicNup98A, N-terminal NIFN repeat domain of, 18 Microfilaments, 182 Micronuclear linker histone (MLH), 18 Micronuclei, 37 Microtubule-dependent mechanism, 21 Microtubule-organizing center (MTOC), 150 Microtubules (MTs), 13, 25, 182 Midblastula transition (MBT), 27 developmental transitions, 24 Mitochondrial gene expression, 10 Mitosis-specific dynamic actin structures (MiDAS), 130 Mitotic progression, 10 Mitotic spindle regulation, 15 Moesin ITAM-like motif, 283 Molecular switches, 225 Rho GTPases, 225 Molluscan hemocytes, 366 Molluscan nudibranch, 378 Molluscan oyster, 378 Monoamine octopamine (OA), 361 Morphogenesis, 257 Mouse embryo fibroblasts, 31 MT See Microtubules (MTs) MT-associated proteins (MAPs), 205 MT-binding proteins, 205 MT-destabilizing proteins, 217 MT-motor proteins, 219 MT-severing protein, 216 MT-stabilizing proteins, 207 plus-end tracking proteins, 211 MT-destabilizing proteins, 217 Capzb2, 219 collapsin response mediator proteins (CRMP), 210 doublecortin (DCX), 209 MAP2, 207 MAP1A, 209 MAP1B, 208 MAPs, 207 SCG-10, 218, 219 stathmin, 218 Tau, 207 MT-motor proteins, 219 dynein-associated proteins, 221 kinesins, 220 MTOC See Microtubule-organizing center (MTOC) MT-severing protein, 216 katanin, 216 spastin, 217 MT-stabilizing proteins, 207 Mucinous ovarian cancer, 34 Multicellular animals, 359 Multidomain proteins, 154 Multi-PDZ domain protein-1 (MUPP-1), 344 Multiple biomechanical sensors, 308 Multiprotein complexes, 127 Murine CAR expression, 330 Muscular dystrophy, 39 Mutator phenotype hypothesis, 36 Myosin M, 145 Mytilus galloprovincialis, 366 N NCAM See Neural cell adhesion molecules (NCAM) NE See Nuclear, envelope (NE) NEBD See Nuclear envelope breakdown (NEBD) 404 Nemertinea, 366 Nemertini, 366 Neotropical fresh-water crab, ventral nerve cord, 371 Nesprin-2 actin binding domain (ABD), 32 C-terminal, 32 KASH domain, 32 mini nuclear size reductions, 32 Neural cell adhesion molecules (NCAM), 202 Neural crest-like cells (NCLC), 375 ascidian Ciona intestinalis, 375 Neuritogenesis, 261 Neuroanatomical phenotypes, 249 Neurohormone, 361 Neuromodulators, 361, 372, 377 Neuronal development, 245 Neuronal morphogenesis, 186 Neuronal network formation, 346 Neuronal trafficking, 259 Neurons, 186 Neurotransmitters, 361, 372 Neurotrophin receptors, 342 Neutrophil differentiation, 32 NF-κB activation, 331 NIMA-related kinases, 13 Niphargus inopinatus, 371 Nitric oxide (NO), 375 NLS See Nuclear, localization signal (NLS) NMCP/LINC/CRWN protein family (nuclear matrix constituent proteins/little nuclei proteins/ crowded nucleus proteins), 21 Nonphosphorylatable valine residue, 304 Noradrenaline, 359 low salinity effects, 369 metabolic pathways of, 360 Norepinephrine, level of, 379 NPC See Nuclear pore complex (NPC) NPFs See Nucleation promoting factors (NPFs) Nuclear cPKC activity, 28 cPKC localization, 16 DNA, envelope (NE), Index expansion, 14 membrane, 36 migration, 36 morphology, 37 defects, transport factorsm, redistribution of, 11 Nuclear, envelope (NE) morphology, Nuclear envelope breakdown (NEBD), 13 starfish oocytes, 13 in vitro Xenopus assay, 13 Nuclear export signal (NES) complex, 10 Nuclear localization signal (NLS), 10 Nuclear pore complex (NPC) A thaliana, 22 insertion, nucleoporin building blocks, 30 nucleoporins (Nups), 10 Nuclear size regulation cell-cycle effects, 13–14 cell size/nucleocytoplasmic ratio, 9–10 cellular structures/activities, overview of, cellular transformation, chromatin state, control nuclear size model organisms and factors, endoplasmic reticulum (ER), 12–13 genome size/ploidy, intranuclear structures, 11 mammalian model systems, 31–32 model systems, to elucidate mechanisms of, 18 Caenorhabditis elegans, 22–24 Daniorerio, 26 Drosophila melanogaster, 24–26 mammalian model systems, 31–32 plant nuclei, 21–22 Tetrahymena thermophila, 18–19 Xenopus, 26–30 yeasts/fungi, 20–21 morphology, functional significance of, 33 cancer, changes, 36–39 chromatin organization, 33–34 chromosome positioning, 33–34 gene expression, 33–34 Index nuclear envelopathies, 39–40 nuclear mechanics/cell migration, 35–36 nucleocytoplasmic transport, 10–11 organelle size control, nuclear structure/models of, signaling pathways, 15–17 Nucleation promoting factors (NPFs), 189 Nucleocytoplasmic transport, 38 Null alleles, 260 Nup136 expression, 22 Nup214 expression, 38 O Octopamine, 360 Octopus vulgaris, 361, 366 Oligochaete, 368 ONM See Outer nuclear membrane (ONM) Ophiopsila aranea, 374 Ophiuroidea, 374 Ostrea edulis, 378 Outer nuclear membrane (ONM), P p21-activated kinase (PAK), 119, 131, 304 PakA, 132 endocytosis, roles in, 133 PakB, 132 endocytosis, roles in, 133 PakC, 134 PakD, 135 PAF See Platelet-activating factor (PAF) Paracellular pathway, 281 PDK See Phosphoinositide-dependent protein kinase (PDK) PDZ-domain-binding motif, 299 PECAM-1 See Platelet endothelial cell adhesion molecule (PECAM-1) Phagocytosis, 152 Phagosomes, 117 Phallusia mammillata, 380 Phallusia nigra, 375 Pharmacological inhibitors, 186 PH–DH–PH region, 155 Phenylethanolamine-N-methyltransferase (PNMT), 360 405 Phestilla sibogae, 378 Phoronis vancouverensis, 378 Phosphatidylinositol 3-kinase (PI3K), 118 Phosphoinositide-dependent protein kinase (PDK), 161 Phosphoinositide 3-kinase (PI3K) signaling, 332 Phosphoinositides, 147 Phosphorylation, 61, 161 serine, 304 Tyr731, 302 Phototaxis defect, 130 Phylum, 366 PI3 kinase activation, 283 PKC phosphorylation, 17 Planorbarius corneus, 366 Planulae, ultrastructural examination of, 377 Platelet-activating factor (PAF), 302 Platelet endothelial cell adhesion molecule (PECAM-1), 298 p53 levels, 34, 38 Plus-end tracking proteins, 211 adenomatous polyposis coli (APC), 214 CLIP-115, 212 CLIP-170, 212 cytoplasmic linker associated protein (CLASP), 213 EB1, 212 EB3, 212 transforming acidic coiled-coil domain family, 216 Pod1 See Polarity osmotic defective-1 (Pod1) Polarity osmotic defective-1 (Pod1), 223 Polychaete, 368 Poly/monoclonal anti-CAR antibodies, 342 Post-MBT embryos, 28 Post-mitotic MT dynamics, 30 Potential signaling, 264 P42/p44 MAPK activation, 348 Presynaptic plasticity, 253 Progeria, 39 Proline-rich tyrosine kinase-2 (Pyk-2), 302 Protein kinase C (PKC), 13, 289 Protein phosphatase γ (PP1γ), 34 406 Protein phosphatase PP2A, 27 Protein–protein interactions, 344 Proteins regulating intracellular trafficking, 343 Protein trafficking, role, 343 CAR signaling, 343 Protein tyrosine phosphatases (PTP) 302, 303 P-selectin glycoprotein ligand-1 (PSGL-1), 280 intracellular domain of, 282 for leukocyte role, 283 mediated signaling, 283 PSGL-1 See P-selectin glycoprotein ligand1 (PSGL-1) PTP See Protein tyrosine phosphatases (PTP) Pycnopodia helianthoides, 374 Pyk2-dependent manner, 289 Q Quorum-sensing molecules, 135 R Rab5 endocytic pathway, 261 Rab proteins, 152 rac genes, 113 expression pattern of, 113 rac1b, 113 rac1c, 113 racF1, 113 racF2, 113 racG, 113 Rac proteins, 113 Rac subfamily Rac1, 117 functional studies on, 118 isoforms of, 118 subcellular localization of, 117 RacB, 118 RacC, 119 actin polymerization, effects on, 119 overexpression of, 119 RacE chemotaxis, role in, 121 cytokinesis, role in, 120 RacF, 121 in sexual cell maturation, 121 Index RacG overexpression of, 122 phagocytosis, roles in, 122 RacH, 122 actin polymerization in vitro, 122 Vacuolin, 122 vesicle trafficking, role in, 122 Radial glial progenitor cells, 13 Ran GTPase activating protein (RanGAP), 10 Ran GTPase cycle, 20 Ran guanine nucleotide exchange factor (RanGEF), 10 Ran nucleocytoplasmic distribution, 11 Rat hippocampal neurons, 268 Rat sympathetic neurons, 264 rdiA gene, disruption, 144 Reactive oxygen species (ROS), 290 Regulatory mechanisms controlling nuclear size, 17 Renilla koellikeri, 362, 365 Repo-Man, 34 Reproduction, 366 Respiration, 366 Reticulon (Rtn), 12 Retinal ganglion cells (RGCs), 193 Retinal pigment epithelial cells, 337 Retinoblastoma (Rb) protein, 38 Reverse-transmigration, 299 RGCs See Retinal ganglion cells (RGCs) RhoA-binding proteins, 124 RhoG activation, 296 RhoGAP–SH3 region, 155 Rho-GEFs Trio, 296 Rho-GTPase, 61, 225, 289, 295 activation cycle, 291 functions, 225 regulators, 225 Rho signaling, 161 pathways, 136, 155 vesicle trafficking, 161, 164 macropinocytosis, 161 phagocytosis, 161 Rho-specific guanine nucleotide dissociation inhibitors (RhoGDIs), 142 functional studies on, 143 407 Index Rhynchocoela, 366 RNAi knockdowns, 24 RNA/protein, membraneless, 11 Roco genes (LRRK2), 148 Roco proteins Roco5, 148 Romanomermis culicivorax, 372 RSC chromatin remodeling complex, 20 RSC mutants, 20 RuvB-like ATPases, 30 S Sabellastarte magni¢ca, 368 Scallops dopamine concentrations, 369 hemolymph, temporal concentration of catecholamines, 370 SCA7 mutant mouse model, 34 Scar complex, 128 cell adhesion, roles in, 130 composition, regulation of, 128 cytokinesis, role in, 130 cytosolic protein, 129 functional studies of, 129 subcellular localization of, 129 vesicle trafficking, role in, 131 Scar/WAVE complex, 138 SCG See Superior cervical ganglia (SCG) Schistosoma japonicum, 364 Sea cucumber, 374 Sea pansy, immunoreactivity in endoderm, 365 Sea snail embryos cytoplasmic partitioning, α-Secretase a disintegrin and metalloprotease (ADAM), 346 Sensory vesicle, dopamine-positive cells, 380 Shrimp, 371 Signaling pathways, Silencing α-actinin-4 decreased endothelial cell stiffness, 295 Slit-Robo GAPS (srGAPs), 153 Slit-Robo-Ras signaling, 194 SNAP25 See Synaptosomal associated protein 25 (SNAP25) SNARE See Soluble N-ethylmaleimidesensitive factor attachment protein receptors (SNARE) Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE), 248 Somatic macronucleus (MAC), 18 Somatic nuclei, Spindle pole bodies (SPBs), 20 NE lipid composition, 20 Src-family kinases, 283 Src homology 2-domain containing tyrosine phosphatase (SHP-2), 302 srGAPs See Slit-Robo GAPS (srGAPs) SUN-domain protein Mps3, 20 Superior cervical ganglia (SCG), 218 Sycon ciliatum, 362 Synapses, 186 Synaptosomal associated protein 25 (SNAP25), 252 Syndapin-like protein (SLP), 124 Syntaxins, 255 T TcTex-1, 223 TeNT See Tetanus neurotoxin (TeNT) Tetanus neurotoxin (TeNT), 249 Tethya wilhelma, 362 Tetrahymena encodes 13 putative importin α-like proteins, 19 Tetrahymena pyriformis, 361 Tetrahymena thermophila, 18 TH-immunoreactive neurons, 371 Tight junctions (TJs), 297 -associated junctional adhesion molecules (JAMs), 299 transmembrane proteins, 298 Tm See Tropomyosins (Tm) Tmod See Tropomodulin (Tmod) Tomosyn, 258 Tpx2 depletion, from Xenopus egg, 30 Transcytosis, 264 Transendothelial migration (TEM), 280 Transforming growth factor beta (TGF-β), 332 Triple CH-domain array exchange factor (Trix), 148 Tropomodulin (Tmod), 199 Tropomyosins (Tm), 199 408 Tubular ER network inhibits nuclear expansion, 12 Tumor necrosis factor alpha (TNF-α), 331 Tunicates, 375 Tyrosine-based motif 318YNQV321, 335 Tyrosine hydroxylase (TH), 360, 372, 380 Tyrosine kinase Src, 289 Tyrosine phosphatase PTP1B, 290 Tyrosine phosphorylation, 294, 302 Tyrosine residues Tyr685, 302 U Urochordates, 375, 380 V Vascular cell adhesion molecule-1 (VCAM-1), 280 VCAM-1 expression, 288 Vascular endothelial growth factor (VEGF), 301 Vasodilator-stimulated phosphoprotein (VASP), 127 VE-cadherin, 298, 300 ADAM10-mediated shedding, 305 -based junctions, 302 C-terminal, 305 -deficient mice, 301 endocytosis, 305 homophilic interactions, 301 inflammatory diseases, 305 intracellular tail of, 301 -mediated adhesion, 303 modulation of, 304 p120-catenin reduces colocalization of, 304 phospho-dependent internalization of, 304 at Ser665, 304 VEGFR3 and R2 signal, 308 Vesicle tethering proteins, 258 Vesicular membrane, 248 Index Vibrio anguillarum, 368 Viral infection, CAR signaling, 347–348 Viral ligands, 348 Virulence factors, 154 Viviparus ater, 366 W WASP See Wiskott-Aldrich syndrome protein (WASP) WASP family proteins, 125 filopodia, 125 lamellipodia, 125 plant trichomes, 125 podosomes, 125 Williams syndrome, 212 Wiskott-Aldrich syndrome, 126 Wiskott-Aldrich syndrome protein (WASP), 114, 189 WASP-B, 128 X Xenopus development nuclear size regulation, 16 Xenopus eggs, 9, 14, 15, 26, 29 Xenopus embryos, 12, 15, 27 Xenopus laevis, 27, 216, 263 Xenopus oocytes germinal vesicle (GV) of, 11 Xenopus tropicalis egg, 27 sperm, 26, 27 Y Yeast studies, Z Zic gene, 375 Zona occludens (ZO) proteins, 290, 298 Zonula occludens (ZO-1) protein, 344 ... Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Daniel L Levy Department of Molecular Biology,. .. Department of Molecular Cell Biology, Sanquin Research and Landsteiner Laboratory, Academic Medical Center, University of Amsterdam, The Netherlands Lidija D Vukovic´ Department of Molecular Biology,. .. University of Rome, Italy Enrico Crivellato Department of Experimental and Clinical Medicine, Section of Anatomy, University of Udine, Italy Anna E Daniel Department of Molecular Cell Biology,