ARHGEF12

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Rho guanine nucleotide exchange factor (GEF) 12
PDB rendering based on 1txd.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols ARHGEF12 ; DKFZp686O2372; KIAA0382; LARG; PRO2792
External IDs Template:OMIM5 Template:MGI HomoloGene9088
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Rho guanine nucleotide exchange factor (GEF) 12, also known as ARHGEF12, 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 a complex with G proteins and stimulate Rho-dependent signals. This protein is observed to form myeloid/lymphoid fusion partner in acute myeloid leukemia.[1]

References

  1. 1.0 1.1 "Entrez Gene: ARHGEF12 Rho guanine nucleotide exchange factor (GEF) 12".

Further reading

  • Nagase T, Ishikawa K, Nakajima D; et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. PMID 9205841.
  • Kourlas PJ, Strout MP, Becknell B; et al. (2000). "Identification of a gene at 11q23 encoding a guanine nucleotide exchange factor: evidence for its fusion with MLL in acute myeloid leukemia". Proc. Natl. Acad. Sci. U.S.A. 97 (5): 2145–50. doi:10.1073/pnas.040569197. PMID 10681437.
  • Fukuhara S, Chikumi H, Gutkind JS (2000). "Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links heterotrimeric G proteins of the G(12) family to Rho". FEBS Lett. 485 (2–3): 183–8. PMID 11094164.
  • Reuther GW, Lambert QT, Booden MA; et al. (2001). "Leukemia-associated Rho guanine nucleotide exchange factor, a Dbl family protein found mutated in leukemia, causes transformation by activation of RhoA". J. Biol. Chem. 276 (29): 27145–51. doi:10.1074/jbc.M103565200. PMID 11373293.
  • Taya S, Inagaki N, Sengiku H; et al. (2002). "Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF". J. Cell Biol. 155 (5): 809–20. doi:10.1083/jcb.200106139. PMID 11724822.
  • Chikumi H, Fukuhara S, Gutkind JS (2002). "Regulation of G protein-linked guanine nucleotide exchange factors for Rho, PDZ-RhoGEF, and LARG by tyrosine phosphorylation: evidence of a role for focal adhesion kinase". J. Biol. Chem. 277 (14): 12463–73. doi:10.1074/jbc.M108504200. PMID 11799111.
  • Perrot V, Vazquez-Prado J, Gutkind JS (2003). "Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF". J. Biol. Chem. 277 (45): 43115–20. doi:10.1074/jbc.M206005200. PMID 12183458.
  • Aurandt J, Vikis HG, Gutkind JS; et al. (2002). "The semaphorin receptor plexin-B1 signals through a direct interaction with the Rho-specific nucleotide exchange factor, LARG". Proc. Natl. Acad. Sci. U.S.A. 99 (19): 12085–90. doi:10.1073/pnas.142433199. PMID 12196628.
  • Hirotani M, Ohoka Y, Yamamoto T; et al. (2002). "Interaction of plexin-B1 with PDZ domain-containing Rho guanine nucleotide exchange factors". Biochem. Biophys. Res. Commun. 297 (1): 32–7. PMID 12220504.
  • Driessens MH, Olivo C, Nagata K; et al. (2002). "B plexins activate Rho through PDZ-RhoGEF". FEBS Lett. 529 (2–3): 168–72. PMID 12372594.
  • Wennerberg K, Ellerbroek SM, Liu RY; et al. (2003). "RhoG signals in parallel with Rac1 and Cdc42". J. Biol. Chem. 277 (49): 47810–7. doi:10.1074/jbc.M203816200. PMID 12376551.
  • 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.
  • Suzuki N, Nakamura S, Mano H, Kozasa T (2003). "Galpha 12 activates Rho GTPase through tyrosine-phosphorylated leukemia-associated RhoGEF". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 733–8. doi:10.1073/pnas.0234057100. PMID 12515866.
  • Chikumi H, Barac A, Behbahani B; et al. (2004). "Homo- and hetero-oligomerization of PDZ-RhoGEF, LARG and p115RhoGEF by their C-terminal region regulates their in vivo Rho GEF activity and transforming potential". Oncogene. 23 (1): 233–40. doi:10.1038/sj.onc.1207012. PMID 14712228.
  • Wang Q, Liu M, Kozasa T; et al. (2004). "Thrombin and lysophosphatidic acid receptors utilize distinct rhoGEFs in prostate cancer cells". J. Biol. Chem. 279 (28): 28831–4. doi:10.1074/jbc.C400105200. PMID 15143072.
  • Kristelly R, Gao G, Tesmer JJ (2004). "Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor". J. Biol. Chem. 279 (45): 47352–62. doi:10.1074/jbc.M406056200. PMID 15331592.
  • Ballif BA, Villén J, Beausoleil SA; et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
  • Okuhira K, Fitzgerald ML, Sarracino DA; et al. (2006). "Purification of ATP-binding cassette transporter A1 and associated binding proteins reveals the importance of beta1-syntrophin in cholesterol efflux". J. Biol. Chem. 280 (47): 39653–64. doi:10.1074/jbc.M510187200. PMID 16192269.
  • Goto M, Muramatsu H, Mihara H; et al. (2006). "Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction". J. Biol. Chem. 280 (49): 40875–84. doi:10.1074/jbc.M507399200. PMID 16192274.
  • Bourguignon LY, Gilad E, Brightman A; et al. (2006). "Hyaluronan-CD44 interaction with leukemia-associated RhoGEF and epidermal growth factor receptor promotes Rho/Ras co-activation, phospholipase C epsilon-Ca2+ signaling, and cytoskeleton modification in head and neck squamous cell carcinoma cells". J. Biol. Chem. 281 (20): 14026–40. doi:10.1074/jbc.M507734200. PMID 16565089.

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