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Rho GTPases and their effector proteins

BISHOP, Anne L., HALL, Alan·2000·Biochemical Journal
DOI 10.1042/bj3480241
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Abstract

Rho GTPases are molecular switches that regulate many essential cellular processes, including actin dynamics, gene transcription, cell-cycle progression and cell adhesion. About 30 potential effector proteins have been identified that interact with members of the Rho family, but it is still unclear which of these are responsible for the diverse biological effects of Rho GTPases. This review will discuss how Rho GTPases physically interact with, and regulate the activity of, multiple effector proteins and how specific effector proteins contribute to cellular responses. To date most progress has been made in the cytoskeleton field, and several biochemical links have now been established between GTPases and the assembly of filamentous actin. The main focus of this review will be Rho, Rac and Cdc42, the three best characterized mammalian Rho GTPases, though the genetic analysis of Rho GTPases in lower eukaryotes is making increasingly important contributions to this field.

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Research works printed but not linked: 10

  1. Ridley, A. J. (2000) Rho. In GTPases (Hall, A., ed.), pp. 89-136, Oxford University Press, Oxford
  2. Debant, A., Serra-Pages, C., Seipel, K., O'Brien, S., Tang, M., Park, S. H. and Streuli, M. (1996) The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. Proc. Natl. Acad. Sci.
  3. Aktories, K.a. K., G. (1997) Clostridium botulinum ADP-ribosyltransferase C3. In Bacterial Toxins : Tools in Cell Biology and Pharmacology (Aktories, K., ed.), pp. 61, Chapman and Hall, Weinheim 33
  4. Aktories, K., Schmidt, G. and Hofmann, F. (2000) GTPases targetted by bacterial toxins. In GTPases (Hall, A., ed.), pp. 311-331, Oxford University Press, Oxford
  5. Takahashi, M., Mukai, H., Toshimori, M., Miyamoto, M. and Ono, Y. (1998) Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. Proc. Natl. Acad. Sci. U.S.A. 95, 11566-11571
  6. Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E. and Pollard, T. D. (1999) Scar, a WASP-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl. Acad. Sci. U.S.A. 96, 3739-3744
  7. Kolluri, R., Tolias, K. F., Carpenter, C. L., Rosen, F. S. and Kirchhausen, T. (1996) Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42. Proc. Natl. Acad. Sci. U.S.A. 93, 5615-5618 157
  8. Ramesh, N., Anton, I. M., Hartwig, J. H. and Geha, R. S. (1997) WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc. Natl. Acad. Sci. U.S.A. 94, 14671-14676 160
  9. Luo, L., Lee, T., Tsai, L., Tang, G., Jan, L. Y. and Jan, Y. N. (1997) Genghis Khan (Gek) as a putative effector for Drosophila Cdc42 and regulator of actin polymerization. Proc. Natl. Acad. Sci. U.S.A. 94, 12963-12968 166
  10. Burbelo, P. D., Snow, D. M., Bahou, W. and Spiegel, S. (1999) MSE55, a Cdc42 effector protein, induces long cellular extensions in fibroblasts. Proc. Natl. Acad.Sci.

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Metadata

Authors
BISHOP, A. L., & HALL, A.
Affiliations
MRC Laboratory for Molecular Cell Biology, University College London, Gower Street, London WC1E 6BT, U.K.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
2000-05-23
Volume
348
Issue
2
Pages
241-255
ISSN
  • 0264-6021
  • 1470-8728
DOI
10.1042/bj3480241
Cited by
2,575
References
2
Language
en

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CoChat. (2026). Citation check: Rho GTPases and their effector proteins. https://app.cochat.ai/papers/10.1042/bj3480241
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BISHOP, A. L., & HALL, A. (2000). Rho GTPases and their effector proteins. Biochemical Journal. https://doi.org/10.1042/bj3480241