ARHGEF12

From Wikipedia, the free encyclopedia

Rho guanine nucleotide exchange factor (GEF) 12

PDB rendering based on 1txd.

Available structures: 1txd, 1x86

Identifiers

Symbol(s)

ARHGEF12; DKFZp686O2372; KIAA0382; LARG; PRO2792

External IDs

OMIM: 604763 MGI: 1916882 HomoloGene: 9088

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

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_015313 (mRNA)
NP_056128 (protein)

NM_027144 (mRNA)
NP_081420 (protein)

Location

Chr 11: 119.71 - 119.87 Mb

n/a

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: ARHGEF12 Rho guanine nucleotide exchange factor (GEF) 12.

[edit] 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.