Abstract
The actin cytoskeleton plays an essential role in many cellular functions, including cell motility and migration, cell division, intracellular transport processes, and phagocytosis. In order to mediate these diverse processes, the actin cytoskeleton is highly dynamic and can be rapidly reorganized in response to a variety of different signals. Actin reorganization is an early response of cells to many growth factors, cytokines and lipid mediators (Ridley 1994). In addition, the composition of the extracellular matrix, the extent of cell spreading and interactions with other cells play an important role in regulating actin organization (Ruoslahti 1997; Schwartz 1997). These different extrinisic signals combine to regulate cellular responses involving the cytoskeleton, and may also induce long-term changes by altering the transcription of cytoskeletal proteins or regulatory proteins. Finally, intrinsic signals during the cell cycle lead to reorganization of actin filaments during mitosis followed by formation and contraction of the actin-based contractile ring at cytokinesis (Ridley 1995).
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References
Adachi H, Takahashi Y, Hasebe T, Shirouzu M, Yokoyama S, Sutoh K (1997) Dictyostelium IQGAP-related protein specifically involved in the completion of cytokinesis. J Cell Biol 137:891–898
Adam T, Giry M, Boquet P, Sansonetti P (1996) Rho-dependent membrane folding causes Shigella entry into epithelial cells. EMBO J 15:3315–3321
Adamson P, Marshall CJ, Hall A, Tilbrook PA (1992a) Post-translational modifications of p21rho proteins. J Biol Chem 267:20033–20038
Adamson P, Paterson HF, Hall A (1992b) Intracellular localization of the p21rho proteins. J Cell Biol 119:617–627
Allen LA, Aderem A (1996) Mechanisms of phagocytosis. Curr Opin Immunol 8:36–40
Allen WE, Jones GE, Pollard JW, Ridley AJ (1997) Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages. J Cell Sci 110:707–720
Araki N, Johnson MT, Swanson JA (1996) A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 135:1249–1260
Aspenström P (1997) A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol 7:479–487
Barbacid M (1987) ras genes. Annu Rev Biochem 56:779–827
Barry ST, Flinn HM, Humphries M, Critchley DR, Ridley AJ (1997) Requirement for Rho in integrin signalling. Cell Adhes Commun 4:387–398
Bashour A-M, Fullerton AT, Hart MJ, Blook GS (1997) IQGAP1, a Rac-and Cdc42-binding protein, directly binds and cross-links microfilaments. J Cell Biol 137:1555–1566
Bourne HA, Sanders DA, McCormick F (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:117–127
Braga VMM, Machesky LM, Hall A, Hotchin NA (1997) The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J Cell Biol 137:1421–1431
Bretscher A, Reczek D, Berryman K (1997) Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci 110:3011–3018
Brock J, Midwinter K, Lewis J, Martin P (1996) Healing of incisional wounds in the embryonic chick wing bud: characterization of the actin purse-string and demonstration of a requirement for Rho activation. J Cell Biol 135:1097–1107
Burridge K, Chrzanowska-Wodnicka M (1996) Focal adhesions, contractility, and signaling. Annu Rev Cell Dev Biol 12:463–519
Bussey H (1996) Cell shape determination: a pivotal role for Rho. Science 272:224–226
Chant J (1996) Generation of cell polarity in yeast. Curr Opin Cell Biol 8:557–565
Chen LM, Hobbie S, Galan JE (1996) Requirement of Cdc42 for Salmonella-induced cytoskeletal and nuclear responses. Science 274:2115–2118
Chrzanowska-Wodnicka M, Burridge K (1996) Rho-stimulated contractility drives the formation of stress fibres and focal adhesions. J Cell Biol 133:1403–1415
Cox D, Chang P, Zhang Q, Reddy PG, Bokoch GM, Greenberg S (1997) Requirements for both Racl and Cdc42 in membrane ruffling and phagocytosis in leukocytes. J Exp Med 186:1487–1494
Cvrcková F, De Virgilio C, Manser E, Pringle JR, Nasmyth K (1995) Ste-20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Genes Dev 9:1817–1830
De Camilli P, Emr SD, McPherson PS, Novick P (1996) Phosphoinositides as regulators in membrane traffic. Science 271:1533–1539
Defilppi P, Olivo C, Tarone G, Mancini P, Rosaria Torrisi M, Eva A (1997) Actin cytoskeleton polymerization in Dbl-transformed NIH3T3 fibroblasts is dependent on cell adhesion to specific extracellular matrix proteins. Oncogene 14:1933–1943
Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R (1989) Rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem 264:16378–16382
Drechsel DN, Hyman AA, Hall A, Glotzer M (1996) A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr Biol 7:12–23
Dutartre H, Davoust J, Gorvel J-P, Chavrier P (1996) Cytokinesis arrest and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase CDC42Hs. J Cell Sci 109:367–377
Eaton S, Auvinen P, Luo L, Jan YN, Simons K (1995) Cdc42 and Racl control different actin-dependent processes in the Drosophila wing disc epithelium. J Cell Biol 131:151–164
Evangelista M, Blundell K, Longtine MS, Chow CJ, Adames J, Pringle JR, Peter M, Boone C (1997) Bnilp, a yeast formin linking Cdc42p and the actin cytoskeleton during polarized morpho-genesis. Science 276:118–122
Faix J, Dittrich W (1996) DGAP1, a homologue of RasGTPawe activatin proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum. FEBS Lett 394:251–257
Fanger GR, Gerwins P, Widmann C, Jarpe MB, Johnson GL (1997) MEKKs, GCKs, MLKs, PAKs, TAKs, and Tpls: upstream regulators of the c-Jun amino-terminal kinases? Curr Opin Genet Dev 7:67–74
Farnsworth CL, Feig LA (1991) Dominant inhibitory mutations in the Mgt+-binding site of RasH prevent its activation by GTP. Mol Cell Biol 11:4822–4829
Fishkind DJ, Wang Y-L (1993) Orientation and three-dimensional organization of actin filaments in dividing cultured cells. J Cell Biol 123:837–848
Flinn HM, Ridley AJ (1996) The small GTP-binding protein Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin. J Cell Sci 109:1133–1141
Foster R, Hu K-Q, Lu Y, Nolan KM, Thissen J, Settleman J (1996) Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation. Mol Cell Biol 16:2689–2699
Freeman JL, Abo A, Lambeth JD (1996) Rac “insert region” is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J Biol Chem 271:19794–19801
Frohman MA, Morris AJ (1996) Rho is only ARF the story. Curr Biol 6:945–947
Habets GGM, Scholtes EHM, Zuydgeest D, van der Kammen RA, Stam JC, Berns A, Collard JG (1994) Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell 77:537–549
Hackam DJ, Rotstein OD, Schreiber A, Zhang WJ, Grinstein S (1997) Rho is required for the initiation of calcium signaling and phagocytosis by Fcy receptors in macrophages. J Exp Med 186:55–66
Hall A (1994) Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu Rev Cell Biol 10:31–54
Hartwig JH, Bokoch GM, Carpenter CL, Janmey PA, Taylor LA, Toker A, Stossel TP (1995) Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643–653
Hirata K, Kikuchi A, Sasaki T, Kuroda S, Kaibuchi K, Matsuura Y, Seki H, Saida K, Takai Y (1992) Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction. J Biol Chem 267:8719–8722
Hirshberg M, Stockley RW, Dodson G, Webb MR (1997) The crystal structure of human racl, a member of the rho-family complexed with a GTP analogue. Nat Struct Biol 4:147–153
Hotchin NA, Hall A (1995) The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J Cell Biol 131:1857–1865
Imamura H, Tanaka K, Hihara T, Umikawa M, Kamei T, Takahashi K, Sasaki T, Takai Y (1997) Bnilp and Bnrlp: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J 16:2745–2755
Jähner D, Hunter T (1991) The ras-related gene rhoB is an immediate-early gene inducible by v-fps, epidermal growth factor and platelet-derived growth factor in rat fibroblasts. Mol Cell Biol 11:3682–3690
Jalink K, van Corven EJ, Hengeveld T, Morii N, Narumiya S, Moolenaar WH (1994) Inhibition of lysophosphatidate-and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein rho. J Cell Biol 126:801–810
Johnson DI, Pringle JR (1990) Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J Cell Biol 111:143–152
Jones BD, Paterson HF, Hall A, Falkow S (1993) Salmonella typhimurium induces membrane ruffling by a growth factor-receptor-independent mechanism. Proc Natl Acad Sci USA 90:10390–10394
Joseph G, Pick E (1996) “Peptide walking” is a novel method for mapping functional domains in proteins. Its application to the Racl-dependent activation of NADPH oxidase. J Biol Chem 270:29079–29082
Kauffmann-Zeh A, Rodriguez-Viciana P, Ulrich E, Gilbert C, Coffer P, Downward J, Evan G (1997) Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB. Nature 385:544–547
Kishi K, Sasaki T, Kuroda S, Itoh T, Takai Y (1993) Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J Cell Biol 120:1187–1195
Kosako H, Amano M, Yanagida M, Tanabe K, Nishi Y, Kaibuchi K, Inagaki M (1997) Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. J Biol Chem 272:10333–10336
Kotani H, Takaishi K, Sasaki T, Takai Y (1997) Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells. Oncogene 14:1705–1713
Kozma R, Sarner S, Ahmed S, Lim L (1997) Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Racl, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol Cell Biol 17:1201–1211
Kreck ML, Freeman JL, Abo A, Lambeth JD (1996) Membrane association of Rac is required for high activity of the respiratory burst oxidase. Biochemistry 35:15683–15692
Lamarche N, Tapon N, Stowers L, Burbelo PD, Aspenström P, Bridges T, Chant J, Hall A (1996) Rac and Cdc42 induce actin polymerization and GI cell cycle progression independently of p65PAK and JNK/SAPK MAP kinase cascade. Cell 87:519–529
Lamaze C, Chuang T-H, Terlecky LJ, Bokoch GM, Schmid SL (1996) Regulation of receptor-mediated endocytosis by Rho and Rac. Nature 382:177–179
Lamoureux P, Altun-Gultekin SF, Lin C, Wagner JA, Heidemann SR (1997) Rac is required for growth cone function but not neurite assembly. J Cell Sci 110:635–641
Lang P, Gesbert F, Delespine-Carmagnat M, Stancou R, Pouchelet M, Bertoglio J (1996) Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J 15:510–519
Larochelle DA, Vithalani KK, De Lozanne A (1996) A novel member of the rho family of small GTP-binding proteins is specifically required for cytokinesis. J Cell Biol 133:1321–1329
Lauffenburger DA, Horwitz AF (1996) Cell migration: a physically integrated molecular process. Cell 84:359–369
Leberer E, Thomas DY, Whiteway M (1997) Pheromone signalling and polarized morphogenesis in yeast. Curr Opin Genet Dev 7:59–66
Lebowitz P, Davide J, Prendergast GC (1995) Evidence that farnesyltransferase inhibitors suppress Ras transformation by interfering with Rho activity. Mol Cell Biol 15:6613–6622
Lebowitz PF, Du W, Prendergast GC (1997) Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription. J Biol Chem 272:16093–16095
Lee S, Escalante R, Firtel RA (1997) A RasGAP is essential for cytokinesis and spatial patterning in Dictyostelium. Development 124:983–996
Lorès P, Morin L, Luna R, Gacon G (1997) Enhanced apoptosis in the thymus of transgenic mice expressing constitutively activated forms of human Rac2GTPase. Oncogene 15:601–605
Machesky LM, Hall A (1996) Rho: a connection between membrane receptor signalling and the actin cytoskeleton. Trends Cell Biol 6:304–310
Machesky LM, Hall A (1997) Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J Cell Biol 138:913–926
Mackay DJG, Esch F, Furthmayr H, Hall A (1997) Rho-and Rac-dependent assembly of focal a dhesion complexes and actin filaments in permeabilized fibroblasts: as essential role for ezrin/ radixin/moesin proteins. J Cell Biol 138:927–938
Malosio ML, Gilardelli D, Paris S, Albertinazzi C, de Curtis I (1997) Differential expression of distinct members of Rho family GTP-binding proteins during neuronal development: identification of Rac1B, a new neural-specific member of the family. J Neurosci 17:6717–6728
Marshall CJ (1993) Protein prenylation: a mediator of protein-protein interactions. Science 259:1865–1866
Miller PJ, Johnson DI (1994) Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe. Mol Cell Biol 14:1075–1083
Mitchison TJ, Cramer LP (1996) Actin-based cell motility and cell locomotion. Cell 84:371–379
Moll J, Sansig G, Fattori E, van der Putten H (1991) The murine racl gene: cDNA cloning, tissue distribution and regulated expression of racl mRNA by disassembly of actin microfilaments. Oncogene 6:863–866
Mólnar A, Theodoras AM, Zon LI, Kyriakis JM (1997) Cdc42Hs, but not Racl, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiring p38/RK. J Biol Chem 272:13229–23235
Morii N, Teru-uchi T, Tominaga T, Kumagai N, Kozaki S, Ushikubi F, Narumiya S (1992) A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation. J Biol Chem 267:20921–20926
Murphy AM, Montell DJ (1996) Cell type-specific roles for Cdc42, Rac and RhoL in Drosophila oogenesis. J Cell Biol 133:617–630
Murphy C, Saffrich R, Grummt M, Gournier H, Rybin V, Rubino M, Auvinen P, Lütcke A, Parton RG, Zerial M (1996) Endosomal dynamics regulated by a Rho protein. Nature 384:427–432
Nishiyama T, Sasaki T, Takaishi K, Masaki K, Hideaki Y, Araki K, Matsuura Y, Takai Y (1994) rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor-and 12–0-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol Cell Biol 14:2447–2456
Nobes CD, Hall A (1995) Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal adhesion complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53–62
Nobes CD, Hawkins P, Stephens L, Hall A (1995) Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J Cell Sci 108:225–233
Norman JC, Price LS, Ridley AJ, Hall A, Koffer A (1994) Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J Cell Biol 126:1005–1015
Norman JC, Price LS, Ridley AJ, Koffer A (1996) The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organisation and exocytosis in mast cells by parallel pathways. Mol Biol Cell 7:1429–1442
Nusrat A, Giry M, Turner JR, Colgan SP, Parkos CA, Carnes D, Lemichez E, Bouquet P, Madara JL (1995) Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia. Proc Natl Acad Sci USA 92:10629–10633
Olofsson B, Chardin P, Touchot N, Zahraoui A, Tavitian A (1988) Expression of the ras-related ralA, rhol2 and rab genes in adult mouse tissues. Oncogene 3:231–234
Olsen MF, Ashworth A, Hall A (1995) An essential role for Rho, Rac and Cdc42 GTPases in cell cycle progression through G,. Science 269:1270–1272
O’Sullivan AJ, Brown AM, Freeman HNM, Gomperts BD (1996) Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O-permeabilized mast cells, as a rac/rhoGDI complex. Mol Biol Cell 7:397–408
Parker P (1995) PI 3-kinase puts GTP on the Rac. Curr Biol 5:577–579
Peppelenbosch MP, Qui R-G, de Vries-Smits AMM, Tertoolen LGJ, de Laat SW, McCormick F, Hall A, Symons MH, Bos JL (1995) Rac mediates growth factor-induced arachidonic acid release. Cell 81:849–856
Price LS, Norman JC, Ridley AJ, Koffer A (1995) Rac and rho as regulators of secretion in mast cells. Curr Biol 5:68–73
Qui R-G, Abo A, McCormick F, Symons M (1997) Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol Cell Biol 17:3449–3463
Quilliam LA, Kato K, Rabun KM, Hisaka MM, Huff SY, Campbell-Burk S, Der CJ (1994) Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors. Mol Cell Biol 14:1113–1121
Ridley AJ (1994) Membrane ruffling and signal transduction. BioEssays 16:321–327
Ridley AJ (1995a) Rho-related proteins: actin cytoskeleton and cell cycle. Curr Opin Genet Dev 5:24–30
Ridley AJ (1995b) Rac and Bcr regulate phagocytic phoxes. Curr Biol 5:710–712
Ridley AJ (1996) Rho: theme and variations. Curr Biol 6:1256–1264
Ridley AJ, Hall A (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:401–410
Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A (1992) The small GTP-binding protein rac regulates growth factor/induced membrane ruffling. Cell 70:401–410
Ridley AJ, Comoglio PM, Hall A (1995) Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac and Rho proteins in MDCK cells. Mol Cell Biol 15:1110–1122
Ruoslahti E (1997) Stretching is good for a cell. Science 276:1345–1346
Salmon ED (1989) Cytokinesis in animal cells. Curr Opin Cell Biol 1:541–547
Schmalzing G, Richter H-P, Hansen A, Schwartz W, Just I, Aktories K (1995) Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes. J Cell Biol 130:1319–1332
Schwartz MA (1997) Integrins, oncogenes and anchorage independence. J Cell Biol 139:575–578
Self AJ, Hall A (1995) Purification of recombination Rho/Rac/G25K from Escherichia coli. Methods Enzymol 256:3–10
Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA (1990) Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein Cdc42. Proc Natl Acad Sci USA 87:9853–9857
Shirsat NV, Pignolo RJ, Kreider BL, Rovera G (1990) A member of the ras gene superfamily is specifically expressed in T, B and myeloid hemopoietic cells. Oncogene 5:769–772
Stossel TP (1993) On the crawling of mammalian cells. Science 260:1086–1094
Symons M (1996) Rho family GTPases: the cytoskeleton and beyond. Trends Biochem Sci 21:178181
Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Tsukita S, Takai Y (1997) Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J Biol Chem 272:23371–23375
Takaishi K, Sasaki T, Kotanin H, Nishioka H, Takai Y (1997) Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J Cell Biol 139:1047–1059
Tapon N, Hall A (1997) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol 9:86–92
Tominaga T, Sugie K, Hirata M, Morii N, Fukata J, Uchida A, Imura H, Narumiya S (1993) Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP-ribosylation of the small molecular weight GTP-binding protein, Rho. J Cell Biol 111:2097–2108
Tsukita S, Yonemura S, Tsukita S (1997) ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci 22:53–58
Vincent S, Jeanteur P, Fort P (1992) Growth-regulated expression of rhoG, a new member of the ras homolog gene family. Mol Cell Biol 12:3138–3148
Watanabe N, Madaule P, Reid T, Ishizaki T, Watanabe GG, Kakizuka A, Saito Y, Nakao K, Jockusch BM, Narumiya S (1997) p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho smal GTPase and is a ligand for profilin. EMBO J 16:3044–3056
Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS (1997) Crystal structure of RhoA-GDP and its functional implicatins. Nat Struct Biol 4:699–703
Welch MD, Holtzman DA, Drubin DG (1994) The yeast actin cytoskeleton. Curr Opin Cell Biol 6:110–119
Welch MD, Mallavarapu A, Rosenblatt J, Mitchison TJ (1997) Actin dynamics in vivo. Curr Opin Cell Biol 9:54–61
Westwick JK, Lambert QT, Clark GJ, Symons M, van Aelst L, Pestell RG, Der CJ (1997) Rac regualtion of transformation, gene expression, and actin organization by multiple, PAKindependent pathways. Mol Cell Biol 17:1324–1335
Wójciak-Stothard B, Entwistle A, Garg R, Ridley AJ (1998) Regulation of TFN-a-induced reorganization of the actin cytoskeleton and cell-cell junctions by Rho, Rac and Cdc42 in human endothelial cells. J Cell Physiol (in press)
Zigmond SH, Joyce M, Borleis J, Bokoch GM, Devreotes PN (1997) Regulation of actin polymerization in cell-free systems by GTPyS and Cdc42. J Cell Biol 138:363–374
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Ridley, A.J. (1999). Rho Family Proteins and Regulation of the Actin Cytoskeleton. In: Jeanteur, P. (eds) Cytoskeleton and Small G Proteins. Progress in Molecular and Subcellular Biology, vol 22. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-58591-3_1
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