ARHGEF2

From Wikipedia, the free encyclopedia

Rho/rac guanine nucleotide exchange factor (GEF) 2

Identifiers

ARHGEF2; P40; DKFZp547L106; DKFZp547P1516; GEF; GEF-H1; GEFH1; KIAA0651; LFP40

External IDs

OMIM: 607560 MGI: 103264 HomoloGene: 3468

Gene ontology
Molecular Function:	• guanyl-nucleotide exchange factor activity • Rho guanyl-nucleotide exchange factor activity • microtubule binding • zinc ion binding • diacylglycerol binding • Rac guanyl-nucleotide exchange factor activity • metal ion binding • Rac GTPase binding
Cellular Component:	• intracellular • microtubule
Biological Process:	• cell morphogenesis • intracellular protein transport • actin filament organization • negative regulation of microtubule depolymerization • intracellular signaling cascade • regulation of Rho protein signal transduction • regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004723 (mRNA)
NP_004714 (protein)

NM_008487 (mRNA)
NP_032513 (protein)

Location

Chr 1: 154.18 - 154.23 Mb

Chr 3: 88.71 - 88.73 Mb

Pubmed search

[1]

[2]

Rho/rac guanine nucleotide exchange factor (GEF) 2, also known as ARHGEF2, is a human gene.^[1]

Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein may form complex with G proteins and stimulate rho-dependent signals.^[1]

[edit] References

^ ^a ^b Entrez Gene: ARHGEF2 rho/rac guanine nucleotide exchange factor (GEF) 2.

[edit] Further reading

Ehrhardt A, Ehrhardt GR, Guo X, Schrader JW (2002). "Ras and relatives--job sharing and networking keep an old family together.". Exp. Hematol. 30 (10): 1089–106. PMID 12384139.
Reddy AB, Chatterjee A, Rothblum LI, et al. (1989). "Isolation and characterization of complementary DNA to proliferating cell nucleolar antigen P40.". Cancer Res. 49 (7): 1763–7. PMID 2466560.
Ishikawa K, Nagase T, Suyama M, et al. (1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.". DNA Res. 5 (3): 169–76. PMID 9734811.
Ren Y, Li R, Zheng Y, Busch H (1999). "Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases.". J. Biol. Chem. 273 (52): 34954–60. PMID 9857026.
Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Gao Y, Xing J, Streuli M, et al. (2002). "Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors.". J. Biol. Chem. 276 (50): 47530–41. doi:10.1074/jbc.M108865200. PMID 11595749.
Krendel M, Zenke FT, Bokoch GM (2002). "Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton.". Nat. Cell Biol. 4 (4): 294–301. doi:10.1038/ncb773. PMID 11912491.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Brajenovic M, Joberty G, Küster B, et al. (2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.". J. Biol. Chem. 279 (13): 12804–11. doi:10.1074/jbc.M312171200. PMID 14676191.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
Zenke FT, Krendel M, DerMardirossian C, et al. (2004). "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor.". J. Biol. Chem. 279 (18): 18392–400. doi:10.1074/jbc.M400084200. PMID 14970201.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336.
Callow MG, Zozulya S, Gishizky ML, et al. (2005). "PAK4 mediates morphological changes through the regulation of GEF-H1.". J. Cell. Sci. 118 (Pt 9): 1861–72. doi:10.1242/jcs.02313. PMID 15827085.
Aijaz S, D'Atri F, Citi S, et al. (2005). "Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition.". Dev. Cell 8 (5): 777–86. doi:10.1016/j.devcel.2005.03.003. PMID 15866167.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006.". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMID 16381901.