RhoC

From Wikipedia, the free encyclopedia


Ras homolog gene family, member C
PDB rendering based on 1a2b.
Available structures: 1a2b, 1cc0, 1cxz, 1dpf, 1ftn, 1kmq, 1lb1, 1ow3, 1s1c, 1tx4, 1x86, 1xcg, 1z2c, 2gcn, 2gco, 2gcp
Identifiers
Symbol(s) RHOC; ARH9; ARHC; H9; MGC1448; MGC61427; RHOH9
External IDs OMIM: 165380 MGI106028 HomoloGene56380
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 389 11853
Ensembl ENSG00000155366 ENSMUSG00000002233
Uniprot P08134 Q62159
Refseq NM_001042678 (mRNA)
NP_001036143 (protein)
NM_007484 (mRNA)
NP_031510 (protein)
Location Chr 1: 113.05 - 113.05 Mb Chr 3: 104.92 - 104.92 Mb
Pubmed search [1] [2]

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, attachment, and motility. [2]

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 proliferation and metastasis. Multiple alternatively spliced variants, encoding the same protein, have been identified.

[edit] References

  1. ^ 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. ISSN 0962-8924. 
  2. ^ a b Entrez Gene: RHOC ras homolog gene family, member C.

[edit] Further reading

  • Wennerberg K, Der CJ (2004). "Rho-family GTPases: it's not only Rac and Rho (and I like it).". J. Cell. Sci. 117 (Pt 8): 1301–12. doi:10.1242/jcs.01118. PMID 15020670. 
  • 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. PMID 1383236. 
  • Chardin P, Madaule P, Tavitian A (1988). "Coding sequence of human rho cDNAs clone 6 and clone 9.". Nucleic Acids Res. 16 (6): 2717. PMID 3283705. 
  • Madaule P, Axel R (1985). "A novel ras-related gene family.". Cell 41 (1): 31–40. PMID 3888408. 
  • Fagan KP, Oliveira L, Pittler SJ (1995). "Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts.". Exp. Eye Res. 59 (2): 235–7. doi:10.1006/exer.1994.1102. PMID 7835413. 
  • Bokoch GM, Bohl BP, Chuang TH (1995). "Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins.". J. Biol. Chem. 269 (50): 31674–9. PMID 7989340. 
  • Morris SW, Valentine MB, Kirstein MN, Huebner K (1993). "Reassignment of the human ARH9 RAS-related gene to chromosome 1p13-p21.". Genomics 15 (3): 677–9. doi:10.1006/geno.1993.1124. PMID 8468062. 
  • Madaule P, Furuyashiki T, Reid T, et al. (1996). "A novel partner for the GTP-bound forms of rho and rac.". FEBS Lett. 377 (2): 243–8. PMID 8543060. 
  • 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. PMID 8662891. 
  • Leung T, Chen XQ, Manser E, Lim L (1996). "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton.". Mol. Cell. Biol. 16 (10): 5313–27. PMID 8816443. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548. 
  • 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. 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. PMID 11839578. 
  • 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. 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. 
  • 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. 
  • Shao F, Dixon JE (2003). "YopT is a cysteine protease cleaving Rho family GTPases.". Adv. Exp. Med. Biol. 529: 79–84. PMID 12756732.