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V-ral simian leukemia viral oncogene homolog A (ras related)
Protein RALA PDB 1u8y.png
PDB rendering based on 1u8y.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RALA ; RAL
External IDs OMIM179550 MGI1927243 HomoloGene3942 GeneCards: RALA Gene
RNA expression pattern
PBB GE RALA 214435 x at tn.png
More reference expression data
Species Human Mouse
Entrez 5898 56044
Ensembl ENSG00000006451 ENSMUSG00000008859
UniProt P11233 P63321
RefSeq (mRNA) NM_005402 NM_019491
RefSeq (protein) NP_005393 NP_062364
Location (UCSC) Chr 7:
39.66 – 39.75 Mb
Chr 13:
17.88 – 17.94 Mb
PubMed search [1] [2]

Ras-related protein Ral-A is a protein that in humans is encoded by the RALA gene.[1][2]


The product of this gene belongs to the small GTPase superfamily, Ras family of proteins. GTP-binding proteins mediate the transmembrane signaling initiated by the occupancy of certain cell surface receptors. This gene encodes a low molecular mass ras-like GTP-binding protein that shares about 50% similarity with other ras proteins.[2]

The direct effects of RalA are uncertain, but it has been shown to play a significant role in filopodia formation[3] and activity-dependent growth of postsynaptic membranes[4] through its interactions with several downstream mediators including the exocyst complex.


RALA has been shown to interact with:


  1. ^ Rousseau-Merck MF, Bernheim A, Chardin P, Miglierina R, Tavitian A, Berger R (Aug 1988). "The ras-related ral gene maps to chromosome 7p15-22". Hum Genet 79 (2): 132–6. doi:10.1007/BF00280551. PMID 3292391. 
  2. ^ a b "Entrez Gene: RALA v-ral simian leukemia viral oncogene homolog A (ras related)". 
  3. ^ Sugihara K, Asano S, Tanaka K, Iwamatsu A, Okawa K, Ohta Y (January 2002). "The exocyst complex binds the small GTPase RalA to mediate filopodia formation". Nat. Cell Biol. 4 (1): 73–8. doi:10.1038/ncb720. PMID 11744922. 
  4. ^ Teodoro RO, Pekkurnaz G, Nasser A, Higashi-Kovtun ME, Balakireva M, McLachlan IG, Camonis J, Schwarz TL (July 2013). "Ral mediates activity-dependent growth of postsynaptic membranes via recruitment of the exocyst". EMBO J. 32 (14): 2039–55. doi:10.1038/emboj.2013.147. PMID 23812009. 
  5. ^ Ohta Y, Suzuki N, Nakamura S, Hartwig JH, Stossel TP (1999). "The small GTPase RalA targets filamin to induce filopodia". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2122–8. doi:10.1073/pnas.96.5.2122. PMC 26747. PMID 10051605. 
  6. ^ Luo JQ, Liu X, Hammond SM, Colley WC, Feig LA, Frohman MA, Morris AJ, Foster DA (1997). "RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1". Biochem. Biophys. Res. Commun. 235 (3): 854–9. doi:10.1006/bbrc.1997.6793. PMID 9207251. 
  7. ^ Kim JH, Lee SD, Han JM, Lee TG, Kim Y, Park JB, Lambeth JD, Suh PG, Ryu SH (1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. 430 (3): 231–5. doi:10.1016/S0014-5793(98)00661-9. PMID 9688545. 
  8. ^ Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA (2003). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976. 
  9. ^ Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH (1995). "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". J. Biol. Chem. 270 (38): 22473–7. doi:10.1074/jbc.270.38.22473. PMID 7673236. 
  10. ^ Cantor SB, Urano T, Feig LA (1995). "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases". Mol. Cell. Biol. 15 (8): 4578–84. PMC 230698. PMID 7623849. 
  11. ^ Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A (1998). "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. 273 (2): 814–21. doi:10.1074/jbc.273.2.814. PMID 9422736. 

Further reading[edit]