Open Access Articles- Top Results for Rnd3


SymbolsRND3 ; ARHE; Rho8; RhoE; memB
External IDsOMIM602924 MGI1921444 HomoloGene21074 GeneCards: RND3 Gene
RNA expression pattern
File:PBB GE RND3 212724 at tn.png
More reference expression data
RefSeq (mRNA)NM_001254738NM_028810
RefSeq (protein)NP_001241667NP_083086
Location (UCSC)Chr 2:
151.32 – 151.4 Mb
Chr 2:
51.13 – 51.15 Mb
PubMed search[1][2]

Rnd3 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases.[1] It is encoded by the gene RND3.[2]

Like other members of the Rho family of Ras-related GTPases it regulates the organization of the actin cytoskeleton in response to extracellular growth factors.


Like Ras, Rho family members appear to cycle between an inactive GDP-bound form and an active GTP-bound form. Three major regulators of Rho activity have been identified: RhoGDIs, which interact with the GDP-bound Rho proteins to keep them in a resting complex (see MIM 601925); GEFs, which promote GDP/GTP exchange leading to activation of Rho proteins (see MIM 601855); and GAPs, which stimulate GTP hydrolysis and return the activated Rho protein to its inactive form (see MIM 602680) (Nobes et al., 1998).[supplied by OMIM][2]


Rnd3 has been shown to interact with ARHGAP5[3] and UBXD5.[4]


  1. ^ Ridley A. (2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends Cell Biol 16 (10): 522–9. PMID 16949823. doi:10.1016/j.tcb.2006.08.006. 
  2. ^ a b "Entrez Gene: RND3 Rho family GTPase 3". 
  3. ^ Wennerberg, Krister; Forget Marie-Annick; Ellerbroek Shawn M; Arthur William T; Burridge Keith; Settleman Jeffrey; Der Channing J; Hansen Steen H (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. (England) 13 (13): 1106–15. ISSN 0960-9822. PMID 12842009. doi:10.1016/S0960-9822(03)00418-4. 
  4. ^ Katoh, Hironori; Harada Amane; Mori Kazutoshi; Negishi Manabu (May 2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Mol. Cell. Biol. (United States) 22 (9): 2952–64. ISSN 0270-7306. PMC 133765. PMID 11940653. doi:10.1128/MCB.22.9.2952-2964.2002. 

Further reading


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