ARHGEF7

From Wikipedia, the free encyclopedia

Rho guanine nucleotide exchange factor (GEF) 7

PDB rendering based on 1by1.

Available structures: 1by1, 1zsg, 2ak5, 2df6, 2esw, 2g6f

Identifiers

Symbol(s)

ARHGEF7; PAK3; BETA-PIX; COOL1; DKFZp761K1021; KIAA0142; KIAA0412; Nbla10314; P50; P50BP; P85; P85COOL1; P85SPR; PIXB

External IDs

OMIM: 605477 MGI: 1860493 HomoloGene: 2895

Gene ontology
Molecular Function:	• guanyl-nucleotide exchange factor activity • Rho guanyl-nucleotide exchange factor activity • protein binding
Cellular Component:	• intracellular
Biological Process:	• signal transduction • regulation of Rho protein signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003899 (mRNA)
NP_003890 (protein)

NM_017402 (mRNA)
NP_059098 (protein)

Location

Chr 13: 110.57 - 110.76 Mb

Chr 8: 11.73 - 11.84 Mb

Pubmed search

[1]

[2]

Rho guanine nucleotide exchange factor (GEF) 7, also known as ARHGEF7, 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 belongs to a family of cytoplasmic proteins that activate the Ras-like family of Rho proteins by exchanging bound GDP for GTP. It may form a complex with G proteins and stimulate Rho-dependent signals. This protein can induce membrane ruffling. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences have not been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: ARHGEF7 Rho guanine nucleotide exchange factor (GEF) 7.

[edit] Further reading

Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression.". Gene 146 (2): 199–207. PMID 8076819.
Nagase T, Seki N, Tanaka A, et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. PMID 8590280.
Oh WK, Yoo JC, Jo D, et al. (1997). "Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion.". Biochem. Biophys. Res. Commun. 235 (3): 794–8. doi:10.1006/bbrc.1997.6875. PMID 9207241.
Manser E, Loo TH, Koh CG, et al. (1998). "PAK kinases are directly coupled to the PIX family of nucleotide exchange factors.". Mol. Cell 1 (2): 183–92. PMID 9659915.
Bagrodia S, Taylor SJ, Jordon KA, et al. (1998). "A novel regulator of p21-activated kinases.". J. Biol. Chem. 273 (37): 23633–6. PMID 9726964.
Turner CE, Brown MC, Perrotta JA, et al. (1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.". J. Cell Biol. 145 (4): 851–63. PMID 10330411.
Bagrodia S, Bailey D, Lenard Z, et al. (1999). "A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins.". J. Biol. Chem. 274 (32): 22393–400. PMID 10428811.
Premont RT, Claing A, Vitale N, et al. (2000). "The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing.". J. Biol. Chem. 275 (29): 22373–80. PMID 10896954.
Ku GM, Yablonski D, Manser E, et al. (2001). "A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT.". EMBO J. 20 (3): 457–65. doi:10.1093/emboj/20.3.457. PMID 11157752.
Koh CG, Tan EJ, Manser E, Lim L (2002). "The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family.". Curr. Biol. 12 (4): 317–21. PMID 11864573.
Brown MC, West KA, Turner CE (2002). "Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway.". Mol. Biol. Cell 13 (5): 1550–65. doi:10.1091/mbc.02-02-0015. PMID 12006652.
Shin EY, Shin KS, Lee CS, et al. (2003). "Phosphorylation of p85 beta PIX, a Rac/Cdc42-specific guanine nucleotide exchange factor, via the Ras/ERK/PAK2 pathway is required for basic fibroblast growth factor-induced neurite outgrowth.". J. Biol. Chem. 277 (46): 44417–30. doi:10.1074/jbc.M203754200. PMID 12226077.
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.
Rosenberger G, Jantke I, Gal A, Kutsche K (2003). "Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling.". Hum. Mol. Genet. 12 (2): 155–67. PMID 12499396.
Park E, Na M, Choi J, et al. (2003). "The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42.". J. Biol. Chem. 278 (21): 19220–9. doi:10.1074/jbc.M301052200. PMID 12626503.
Mignone F, Grillo G, Liuni S, Pesole G (2003). "Computational identification of protein coding potential of conserved sequence tags through cross-species evolutionary analysis.". Nucleic Acids Res. 31 (15): 4639–45. PMID 12888525.
Yamamoto Y, Fujimoto Y, Arai R, et al. (2003). "Retrotransposon-mediated restoration of Chlorella telomeres: accumulation of Zepp retrotransposons at termini of newly formed minichromosomes.". Nucleic Acids Res. 31 (15): 4646–53. PMID 12888526.
Flanders JA, Feng Q, Bagrodia S, et al. (2003). "The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins.". FEBS Lett. 550 (1-3): 119–23. PMID 12935897.
Shin EY, Woo KN, Lee CS, et al. (2004). "Basic fibroblast growth factor stimulates activation of Rac1 through a p85 betaPIX phosphorylation-dependent pathway.". J. Biol. Chem. 279 (3): 1994–2004. doi:10.1074/jbc.M307330200. PMID 14557270.
Lim CS, Kim SH, Jung JG, et al. (2004). "Regulation of SPIN90 phosphorylation and interaction with Nck by ERK and cell adhesion.". J. Biol. Chem. 278 (52): 52116–23. doi:10.1074/jbc.M310974200. PMID 14559906.