Rnd2

From Wikipedia, the free encyclopedia


Rho family GTPase 2
Identifiers
Symbol(s) RND2; ARHN; RHO7; RhoN
External IDs OMIM: 601555 MGI1338755 HomoloGene21123
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 8153 11858
Ensembl ENSG00000108830 ENSMUSG00000001313
Uniprot P52198 Q3B842
Refseq NM_005440 (mRNA)
NP_005431 (protein)
NM_009708 (mRNA)
NP_033838 (protein)
Location Chr 17: 38.43 - 38.43 Mb Chr 11: 101.28 - 101.29 Mb
Pubmed search [1] [2]

Rnd2 is a small (~21 kDa) signaling G protein (more specifically a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases.[1]. It is encoded by the gene RND2.[2]

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM][2]

This particular family member has been implicated in the regulation of neuronal morphology and endosomal trafficking.

The gene localizes to chromosome 17 and is the centromeric neighbor of the breast-ovarian cancer susceptibility gene BRCA1.[2]

[edit] References

  1. ^ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol 16 (10): 522-9. ISSN 0962-8924. 
  2. ^ a b c Entrez Gene: RND2 Rho family GTPase 2.

[edit] Further reading

  • Chardin P (1991). "Small GTP-binding proteins of the ras family: a conserved functional mechanism?". Cancer Cells 3 (4): 117-26. PMID 1909153. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548. 
  • Smith TM, Lee MK, Szabo CI, et al. (1997). "Complete genomic sequence and analysis of 117 kb of human DNA containing the gene BRCA1.". Genome Res. 6 (11): 1029-49. PMID 8938427. 
  • Nobes CD, Lauritzen I, Mattei MG, et al. (1998). "A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion.". J. Cell Biol. 141 (1): 187-97. PMID 9531558. 
  • Tanaka H, Fujita H, Katoh H, et al. (2002). "Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2.". Biochem. J. 365 (Pt 2): 349-53. doi:10.1042/BJ20020062. PMID 11931639. 
  • Katoh H, Harada A, Mori K, Negishi M (2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers.". Mol. Cell. Biol. 22 (9): 2952-64. PMID 11940653. 
  • Fujita H, Katoh H, Ishikawa Y, et al. (2003). "Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching.". J. Biol. Chem. 277 (47): 45428-34. doi:10.1074/jbc.M208090200. PMID 12244061. 
  • 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. 
  • Naud N, Touré A, Liu J, et al. (2003). "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male germ cells.". Biochem. J. 372 (Pt 1): 105-12. doi:10.1042/BJ20021652. PMID 12590651. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173-8. doi:10.1038/nature04209. PMID 16189514. 
  • Kim YS, Hori M, Yasuda K, Ozaki H (2006). "Differences in the gestational pattern of mRNA expression of the Rnd family in rat and human myometria.". Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 142 (4): 410-5. doi:10.1016/j.cbpa.2005.08.028. PMID 16311049. 
  • Tanaka H, Katoh H, Negishi M (2006). "Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity.". J. Biol. Chem. 281 (15): 10355-64. doi:10.1074/jbc.M511314200. PMID 16481321.