Rho-family GTPases: it's not only Rac and Rho (and I like it)

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Rho-family GTPases : it's not only Rac and Rho (and I like it). / Wennerberg, Krister; Der, Channing J.

In: Journal of Cell Science, Vol. 117, No. Pt 8, 15.03.2004, p. 1301-12.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Wennerberg, K & Der, CJ 2004, 'Rho-family GTPases: it's not only Rac and Rho (and I like it)', Journal of Cell Science, vol. 117, no. Pt 8, pp. 1301-12. https://doi.org/10.1242/jcs.01118

APA

Wennerberg, K., & Der, C. J. (2004). Rho-family GTPases: it's not only Rac and Rho (and I like it). Journal of Cell Science, 117(Pt 8), 1301-12. https://doi.org/10.1242/jcs.01118

Vancouver

Wennerberg K, Der CJ. Rho-family GTPases: it's not only Rac and Rho (and I like it). Journal of Cell Science. 2004 Mar 15;117(Pt 8):1301-12. https://doi.org/10.1242/jcs.01118

Author

Wennerberg, Krister ; Der, Channing J. / Rho-family GTPases : it's not only Rac and Rho (and I like it). In: Journal of Cell Science. 2004 ; Vol. 117, No. Pt 8. pp. 1301-12.

Bibtex

@article{bda42c3b65274192a77c2500a0876325,
title = "Rho-family GTPases: it's not only Rac and Rho (and I like it)",
abstract = "The Rho-family proteins make up a major branch of the Ras superfamily of small GTPases. To date, 22 human genes encoding at least 25 proteins have been described. The best known 'classical' members are RhoA, Rac1 and Cdc42. Highly related isoforms of these three proteins have not been studied as intensively, in part because it has been assumed that they are functionally identical to their better-studied counterparts. This now appears not to be the case. Variations in C-terminal-signaled modifications and subcellular targeting cause otherwise highly biochemically related isoforms (e.g. RhoA, RhoB and RhoC) to exhibit surprisingly divergent biological activities. Whereas the classical Rho GTPases are regulated by GDP/GTP cycling, other Rho GTPases are also regulated by other mechanisms, particularly by transcriptional regulation. Newer members of the family possess additional sequence elements beyond the GTPase domain, which suggests they exhibit yet other mechanisms of regulation.",
keywords = "Amino Acid Motifs, Amino Acid Sequence, Gene Expression Regulation, Enzymologic, Humans, Models, Biological, Molecular Sequence Data, Phylogeny, Protein Processing, Post-Translational, Protein Structure, Tertiary, Sequence Homology, Amino Acid, cdc42 GTP-Binding Protein/genetics, rac1 GTP-Binding Protein/genetics, rho GTP-Binding Proteins/chemistry, rhoA GTP-Binding Protein/genetics",
author = "Krister Wennerberg and Der, {Channing J}",
year = "2004",
month = mar,
day = "15",
doi = "10.1242/jcs.01118",
language = "English",
volume = "117",
pages = "1301--12",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",
number = "Pt 8",

}

RIS

TY - JOUR

T1 - Rho-family GTPases

T2 - it's not only Rac and Rho (and I like it)

AU - Wennerberg, Krister

AU - Der, Channing J

PY - 2004/3/15

Y1 - 2004/3/15

N2 - The Rho-family proteins make up a major branch of the Ras superfamily of small GTPases. To date, 22 human genes encoding at least 25 proteins have been described. The best known 'classical' members are RhoA, Rac1 and Cdc42. Highly related isoforms of these three proteins have not been studied as intensively, in part because it has been assumed that they are functionally identical to their better-studied counterparts. This now appears not to be the case. Variations in C-terminal-signaled modifications and subcellular targeting cause otherwise highly biochemically related isoforms (e.g. RhoA, RhoB and RhoC) to exhibit surprisingly divergent biological activities. Whereas the classical Rho GTPases are regulated by GDP/GTP cycling, other Rho GTPases are also regulated by other mechanisms, particularly by transcriptional regulation. Newer members of the family possess additional sequence elements beyond the GTPase domain, which suggests they exhibit yet other mechanisms of regulation.

AB - The Rho-family proteins make up a major branch of the Ras superfamily of small GTPases. To date, 22 human genes encoding at least 25 proteins have been described. The best known 'classical' members are RhoA, Rac1 and Cdc42. Highly related isoforms of these three proteins have not been studied as intensively, in part because it has been assumed that they are functionally identical to their better-studied counterparts. This now appears not to be the case. Variations in C-terminal-signaled modifications and subcellular targeting cause otherwise highly biochemically related isoforms (e.g. RhoA, RhoB and RhoC) to exhibit surprisingly divergent biological activities. Whereas the classical Rho GTPases are regulated by GDP/GTP cycling, other Rho GTPases are also regulated by other mechanisms, particularly by transcriptional regulation. Newer members of the family possess additional sequence elements beyond the GTPase domain, which suggests they exhibit yet other mechanisms of regulation.

KW - Amino Acid Motifs

KW - Amino Acid Sequence

KW - Gene Expression Regulation, Enzymologic

KW - Humans

KW - Models, Biological

KW - Molecular Sequence Data

KW - Phylogeny

KW - Protein Processing, Post-Translational

KW - Protein Structure, Tertiary

KW - Sequence Homology, Amino Acid

KW - cdc42 GTP-Binding Protein/genetics

KW - rac1 GTP-Binding Protein/genetics

KW - rho GTP-Binding Proteins/chemistry

KW - rhoA GTP-Binding Protein/genetics

U2 - 10.1242/jcs.01118

DO - 10.1242/jcs.01118

M3 - Review

C2 - 15020670

VL - 117

SP - 1301

EP - 1312

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - Pt 8

ER -

ID: 199432957