N-terminal Dbl domain of the RhoGEF, Kalirin.

Document Type

Article

Publication Date

3-2012

Publication Title

Journal of Biomolecular NMR

Volume

52

Issue

3

First page number:

269

Last page number:

276

Abstract

Guanine nucleotide exchange factors (GEF) promote the release of GDP from GTPases, thus allowing the free GTPase molecule to bind the more abundant GTP molecule. In the GTP-bound state, the GTPase elicits signal transduction by acting on its effector proteins. Spontaneous release of GDP is a slow process and the catalysis of the GDP release by a GEF is generally a prerequisite for efficient signaling (Vetter and Wittinghofer 2001). The structurally related GEFs form subfamilies that regulate a specific family of GTPase proteins. GEFs that activate Rho GTPases have been implicated in cancer and mental retardation. RhoGEFs are a relatively large family, and many of the *69 human RhoGEFs were discovered based on their oncogenic activation in cancer and cancer models. The catalytic components of RhoGEFs are referred to as Dbl homology domains, after the screen that identified the protein Dbl encoded by the diffuse B-cell lymphoma (dbl) oncogene (Eva and Aaronson 1985). Thus the RhoGEF family is a potential target for treating tumors and cancer.

Keywords

Cancer; Cancer—Treatment; G proteins; Guanine Nucleotide Exchange Factors/chemistry; Nuclear Magnetic Resonance; Biomolecular/methods; Proteins—Structure; Protein Structure; Tertiary; Tumors

Disciplines

Life Sciences

Language

English

Find It

UNLV article access

Search your library

Share

COinS