A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion

Journal of Cell Biology

Volumn 141, Issue 1, 1998, Pages 187-197

  Nobes, Catherine D ^c   Lauritzen, Inger ^a   Mattei, Marie Geneviève ^b   Paris, Sonia ^a   Hall, Alan ^c   Chardin, Pierre ^a,d  

^a CNRS   (France)

^b TIMONE HOSPITAL   (France)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

ACTIN FILAMENT; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL ADHESION; CELLULAR DISTRIBUTION; CYTOSKELETON; ENZYME ACTIVITY; ENZYME LOCALIZATION; EPITHELIUM CELL; FIBROBLAST; GROWTH REGULATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY;

3T3 CELLS; ACTINS; AMINO ACID SEQUENCE; ANIMALS; BRAIN; CATTLE; CELL ADHESION; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN; CHROMOSOMES, HUMAN, PAIR 12; CHROMOSOMES, HUMAN, PAIR 17; DNA, COMPLEMENTARY; FIBROBLASTS; GENE LIBRARY; GTP PHOSPHOHYDROLASES; GTP-BINDING PROTEINS; HUMANS; IN SITU HYBRIDIZATION; KINETICS; LIVER; LYMPHOCYTES; MALE; MICE; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; RECOMBINANT PROTEINS; RHO GTP-BINDING PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TESTIS;

EID: 0032489841     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.1.187     Document Type: Article

References (30)

1. Aberle, H., C. Bierkamp, D. Torchard, O. Serova, T. Wagner, E. Natt, J. Wirshing, C. Heidkamper, M. Montagna, H.T. Lynch, et al. 1995. The human plakoglobin gene localizes on chromosome 17 q21 and is subjected to loss of heterozygosity in breast and ovarian cancers. Proc. Natl. Acad. Sci. USA. 92:6384-6388.
2. Aktories, K., and Just, I. 1995. In vitro ADP-ribosylation of Rho by bacterial ADP-ribosyl transferases. Methods Enzymol. 256:184-195.
3. Amano, M., M. Ito, K. Kimura, Y. Fukata, K. Chihara, T. Nakano, Y. Matsuura, and K. Kaibuchi. 1996. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271:20246-20249.
4. Bar-Sagi D., and J.R. Feramisco. 1986. Induction of membrane ruffling and fluid-phase pinocytosis in quiescent fibroblasts by Ras proteins. Science. 233:1061-1068.
5. Cerione, R.A., and Y. Zheng. 1996. The Dbl family of oncogenes. Curr. Opin. Cell Biol. 8:216-222.
6. Chardin, P., P. Boquet, P. Madaule, M.R. Popoff, E.J. Rubin and D.M. Gill. 1989. The mammalian G protein RhoC is ADP-ribosylated by clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO (Eur. Mol. Biol. Organ.) J. 8:1087-1092.
7. Coso, O.A., M. Chiariello, J.C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and, J.S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell. 81:1137-1146.
8. Der, C.J., T. Finkel, and G.M. Cooper. 1986. Biological and biochemical properties of human Hras genes mutated at codon 61. Cell. 44:167-176.
9. Foster, R., K.-Q. Hu, Y. Lu, K.M. Nolan, J. Thissen, and J. Settleman. 1996. Identification of a novel human Rho protein with unusual properties: GT-Pase deficiency and in-vivo farnesylation. Mol. Cell. Biol. 16:2689-2699.
10. Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science. 279:509-514.
11. Huber, L.A., O. Ullrich, Y. Takai, A. Lutcke, P. Dupree, V. Olkkonen, H. Virtta, M.J. Dehoop, K. Alexandrov, M. Peter, M. Zerial, and K. Simons. 1994. Mapping of Ras-related GTP-binding proteins by GTP overlay following two-dimensional gel electrophoresis. Proc. Natl. Acad. Sci. USA. 91:7874-7878.
12. Hughes, P.E., M.W. Renshaw, M. Pfaff, J. Forsyth, V.M. Keivens, M.A. Schwartz, and M.H. Ginsberg. 1997. Suppression of integrin activation: a novel function of a Ras/raf-initiated MAP kinase pathway. Cell. 88:521-530.
13. John, J., M. Frech, and A. Wittinghofer. 1988. Biochemical properties of H-Ras encoded p21 mutants and mechanism of the autophosphorylation reaction. J. Biol. Chem. 263:11792-11799.
14. Kimura, K., M. Ito, M. Amano, K. Chihara, Y. Fukata, M. Nakafuka, B. Yamamori, J. Feng, T. Nakano, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1996. Regulation of myosin phosphatase by Rho and Rho-associated kinase. Science. 273:245-248.
15. Kozma, R., S. Ahmed, A. Best, and L. Lim. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1942-1952.
16. Lamarche, N., and A. Hall. 1994. GAPs for Rho-related GTPases. Trends Genet. 10:436-440.
17. Leung, T., X.Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
18. Lloyd, A.C., H.F. Paterson, J.D. Morris, A. Hall and C.J. Marshall. 1989. p21H-ras-induced morphological transformation and increases in c-myc expression are independent of protein kinase C. EMBO (Eur. Mol. Biol. Organ.) J. 8:1099-1104.
19. Mackay, D.J.G., F. Esch, H. Furthmayr, and A. Hall. 1997. Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role fr ezrin/radixin/moesin proteins. J. Cell Biol. 138:927-938.
20. Minden, A., A. Lin, F.X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 81:1147-1157.
21. Nobes, C.D., and A. Hall. 1995. Rho, rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:53-62.
22. Pai, E.F., U. Krengel, G.A. Petsko, R.S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO (Eur. Mol. Biol. Organ.) J. 9:2351-2359.
23. Prendergast, G.C., J.P. Davide, S.J. Desolms, E.A. Guiliani, S.L. Graham, J.B. Gibbs, A. Oliff, and N.E. Kohl. 1994. Farnesyltransferase inhibition causes morphological reversion of Ras-transformed cells by a complex mechanism that involves regulation of the actin cytoskeleton. Mol. Cell. Biol. 14:4193-4202.
24. Qiu, R.-G., J. Chen, F. McCormick, and M. Symons. 1995. A role for Rho in Ras transformation. Proc. Natl. Acad. Sci. USA. 92:11781-11785.
25. Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:389-399.
26. Ridley, A.J., H.F. Patterson, C.L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell. 70:401-410.
27. Smith, T.M., M.K. Lee, C.I. Szabo, N. Jerome, M. McEven, M. Taylor, L. Hood, and M.C. King. 1996. Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1. Genome Research. 6:1029-1049.
28. Tsukita, Sa., S. Yonemura, and Sh. Tsukita. 1997. ERM family: from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9:70-75.
29. Ueda, T., A. Kikuchi, N. Ohga, J. Yamamoto, and Y. Takai. 1990. Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein. J. Biol. Chem. 265:9373-9380.
30. Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.