RhoC

Ras homolog gene family, member C
	; PDB rendering based on 1a2b.
Available structures
PDB	1Z2C, 2GCN, 2GCO
Identifiers
Symbols	RHOC; ARH9; ARHC; H9; MGC1448; MGC61427; RHOH9
External IDs	OMIM: 165380 MGI: 106028 HomoloGene: 90945 GeneCards: RHOC Gene
Gene Ontology
Molecular function	• nucleotide binding; • GTPase activity; • signal transducer activity; • protein binding; • GTP binding; • protein domain specific binding;
Cellular component	• intracellular; • membrane fraction; • soluble fraction; • nucleus; • cytoplasm; • cytosol; • plasma membrane; • plasma membrane; • axon;
Biological process	• response to hypoxia; • GTP catabolic process; • signal transduction; • small GTPase mediated signal transduction; • axon guidance; • regulation of actin polymerization or depolymerization; • response to mechanical stimulus; • response to glucose stimulus; • positive regulation of cell growth; • positive regulation of cell migration; • positive regulation of actin filament polymerization; • stress-activated protein kinase signaling cascade; • response to drug; • positive regulation of I-kappaB kinase/NF-kappaB cascade; • negative regulation of I-kappaB kinase/NF-kappaB cascade; • response to amino acid stimulus; • positive regulation of caspase activity; • positive regulation of neuron apoptosis; • response to ethanol; • negative regulation of neuron differentiation; • positive regulation of translation; • positive regulation of cell adhesion; • positive regulation of vasoconstriction; • neuron projection morphogenesis; • regulation of dendrite development; • regulation of small GTPase mediated signal transduction; • response to glucocorticoid stimulus; • negative regulation of calcium ion transport via voltage-gated calcium channel activity;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

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RhoC (Ras homolog gene family, member C) is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rac subfamily of the family Rho family of GTPases.^[1] It is encoded by the gene RHOC. ^[2]

[edit] Mechanism and function

It cycles between inactive GDP-bound and active GTP-bound states and function as molecular switches in signal transduction cascades. Rho proteins promote reorganization of the actin cytoskeleton and regulate cell shape and motility. RhoC can activate formins such as mDia1 and FMNL2 to remodel the cytoskelton.^[3]

It is prenylated at its C-terminus, and localizes to the cytoplasm and plasma membrane. It is thought to be important in cell locomotion. Overexpression of this gene is associated with tumor cell invasion and metastasis. RhoC-deficient mice can still develop tumors but these fail to metastasize, arguing that RhoC is essential for metastasis.^[4]

[edit] References

^ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
^ "Entrez Gene: RHOC ras homolog gene family, member C". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=389.
^ Kitzing TM, Wang Y, Pertz O, Copeland JW, Grosse R (April 2010). "Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC". Oncogene 29 (16): 2441–8. doi:10.1038/onc.2009.515. PMID 20101212.
^ Hakem A, Sanchez-Sweatman O, You-Ten A, Duncan G, Wakeham A, Khokha R, Mak TW (September 2005). "RhoC is dispensable for embryogenesis and tumor initiation but essential for metastasis". Genes Dev. 19 (17): 1974–9. doi:10.1101/gad.1310805. PMC 1199568. PMID 16107613. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1199568.

[edit] Further reading

Wheeler AP, Ridley AJ (2004). "Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility.". Exp. Cell Res. 301 (1): 43–9. doi:10.1016/j.yexcr.2004.08.012. PMID 15501444.
Adamson P, Paterson HF, Hall A (1992). "Intracellular localization of the P21rho proteins.". J. Cell Biol. 119 (3): 617–27. doi:10.1083/jcb.119.3.617. PMC 2289677. PMID 1383236. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2289677.
Chardin P, Madaule P, Tavitian A (1988). "Coding sequence of human rho cDNAs clone 6 and clone 9.". Nucleic Acids Res. 16 (6): 2717. doi:10.1093/nar/16.6.2717. PMC 336400. PMID 3283705. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=336400.
Madaule P, Axel R (1985). "A novel ras-related gene family.". Cell 41 (1): 31–40. doi:10.1016/0092-8674(85)90058-3. PMID 3888408.
Reid T, Furuyashiki T, Ishizaki T, et al. (1996). "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain.". J. Biol. Chem. 271 (23): 13556–60. doi:10.1074/jbc.271.23.13556. PMID 8662891.
Maekawa M, Ishizaki T, Boku S, et al. (1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase.". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159.
Clark EA, Golub TR, Lander ES, Hynes RO (2000). "Genomic analysis of metastasis reveals an essential role for RhoC.". Nature 406 (6795): 532–5. doi:10.1038/35020106. PMID 10952316.
Diviani D, Soderling J, Scott JD (2001). "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.". J. Biol. Chem. 276 (47): 44247–57. doi:10.1074/jbc.M106629200. PMID 11546812.
Kleer CG, van Golen KL, Zhang Y, et al. (2002). "Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability.". Am. J. Pathol. 160 (2): 579–84. PMC 1850656. PMID 11839578. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1850656.
van Golen KL, Bao LW, Pan Q, et al. (2002). "Mitogen activated protein kinase pathway is involved in RhoC GTPase induced motility, invasion and angiogenesis in inflammatory breast cancer.". Clin. Exp. Metastasis 19 (4): 301–11. doi:10.1023/A:1015518114931. PMID 12090470.
Arthur WT, Ellerbroek SM, Der CJ, et al. (2003). "XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC.". J. Biol. Chem. 277 (45): 42964–72. doi:10.1074/jbc.M207401200. PMID 12221096.
Shao F, Dixon JE (2003). "YopT is a cysteine protease cleaving Rho family GTPases.". Adv. Exp. Med. Biol. 529: 79–84. doi:10.1007/0-306-48416-1_14. PMID 12756732.