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Rho GTPases and signaling networks

Open access
Van Aelst, Linda, D’Souza-Schorey, Crislyn·1997·Genes & Development

Abstract

The Rho GTPases form a subgroup of the Ras superfamily of 20- to 30-kD GTP-binding proteins that have been shown to regulate a wide spectrum of cellular functions. These proteins are ubiquitously expressed across the species, from yeast to man. The mammalian Rho-like GTPases comprise at least 10 distinct proteins: RhoA, B, C, D, and E; Rac1 and 2; RacE; Cdc42Hs, and TC10. A comparison of the amino acid sequences of the Rho proteins from various species has revealed that they are conserved in primary structure and are 50%–55% homologous to each other. Like all members of the Ras superfamily, the Rho GTPases function as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state. Until recently, members of the Rho subfamily were believed to be involved primarily in the regulation of cytoskeletal organization in response to extracellular growth factors. However, research from a number of laboratories over the past few years has revealed that the Rho GTPases play crucial roles in diverse cellular events such as membrane trafficking, transcriptional regulation, cell growth control, and development. Consequently, a major challenge has been to unravel the underlying molecular mechanisms by which the Rho GTPases mediate these various activities. Many targets of the Rho GTPases have now been identified and further characterization of some of them has provided major insights toward our understanding of Rho GTPase function at the molecular level. This review aims to summarize the general established principles about the Rho GTPases and some of the more recent exciting findings, hinting at novel, unanticipated functions of the Rho GTPases.

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Crossref · 10.1101/gad.11.18.2295

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Cites

  • Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms

    Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555 · cited 2×

    “Direct activators of JNK and p38 are either the dual specificity kinase SEK1 (also called MEKK4 or JNKK), which activates both JNK and p38 when overexpressed, or MKK3 and MKK6 which specifically activate p38 (Sanchez et al. 1994; Derijard et al. 1995; Han et al. 1996; Jiang et al. 1996; Raingeaud et al. 1996).”
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Metadata

Authors
Van Aelst, L., & D’Souza-Schorey, C.
Venue
Genes & Development
Published
1997-09-15
Volume
11
Issue
18
Pages
2295-2322
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2077792958
Cited by
2,358
References
1
Type
posted content
Language
en
Open access
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