RALA
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]
Interactions
RALA has been shown to interact with Filamin,[3] Phospholipase D1[4][5] and RALBP1.[6][7][8][9]
References
- ^ 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.
- ^ a b "Entrez Gene: RALA v-ral simian leukemia viral oncogene homolog A (ras related)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5898.
- ^ Ohta, Y; Suzuki N, Nakamura S, Hartwig J H, Stossel T P (Mar. 1999). "The small GTPase RalA targets filamin to induce filopodia". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (5): 2122–8. doi:10.1073/pnas.96.5.2122. ISSN 0027-8424. PMC 26747. PMID 10051605. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26747.
- ^ Luo, J Q; Liu X, Hammond S M, Colley W C, Feig L A, Frohman M A, Morris A J, Foster D A (Jun. 1997). "RalA interacts directly with the Arf-responsive, PIP2-dependent phospholipase D1". Biochem. Biophys. Res. Commun. (UNITED STATES) 235 (3): 854–9. doi:10.1006/bbrc.1997.6793. ISSN 0006-291X. PMID 9207251.
- ^ Kim, J H; Lee S D, Han J M, Lee T G, Kim Y, Park J B, Lambeth J D, Suh P G, Ryu S H (Jul. 1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. (NETHERLANDS) 430 (3): 231–5. doi:10.1016/S0014-5793(98)00661-9. ISSN 0014-5793. PMID 9688545.
- ^ Moskalenko, Serge; Tong Chao, Rosse Carine, Mirey Gladys, Formstecher Etienne, Daviet Laurent, Camonis Jacques, White Michael A (Dec. 2003). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. (United States) 278 (51): 51743–8. doi:10.1074/jbc.M308702200. ISSN 0021-9258. PMID 14525976.
- ^ Jullien-Flores, V; Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis J H (Sep. 1995). "Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity". J. Biol. Chem. (UNITED STATES) 270 (38): 22473–7. doi:10.1074/jbc.270.38.22473. ISSN 0021-9258. PMID 7673236.
- ^ Cantor, S B; Urano T, Feig L A (Aug. 1995). "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases". Mol. Cell. Biol. (UNITED STATES) 15 (8): 4578–84. ISSN 0270-7306. PMC 230698. PMID 7623849. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230698.
- ^ Ikeda, M; Ishida O, Hinoi T, Kishida S, Kikuchi A (Jan. 1998). "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral". J. Biol. Chem. (UNITED STATES) 273 (2): 814–21. doi:10.1074/jbc.273.2.814. ISSN 0021-9258. PMID 9422736.
Further reading
- Kinsella BT, Erdman RA, Maltese WA (1991). "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA". J. Biol. Chem. 266 (15): 9786–94. PMID 1903399.
- Polakis PG, Weber RF, Nevins B, et al. (1989). "Identification of the ral and rac1 gene products, low molecular mass GTP-binding proteins from human platelets". J. Biol. Chem. 264 (28): 16383–9. PMID 2550440.
- Chardin P, Tavitian A (1989). "Coding sequences of human ralA and ralB cDNAs". Nucleic Acids Res. 17 (11): 4380. doi:10.1093/nar/17.11.4380. PMC 317954. PMID 2662142. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=317954.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230698.
- Jullien-Flores V, Dorseuil O, Romero F, et al. (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.
- Wang KL, Khan MT, Roufogalis BD (1997). "Identification and characterization of a calmodulin-binding domain in Ral-A, a Ras-related GTP-binding protein purified from human erythrocyte membrane". J. Biol. Chem. 272 (25): 16002–9. doi:10.1074/jbc.272.25.16002. PMID 9188503.
- Luo JQ, Liu X, Hammond SM, et al. (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.
- Ikeda M, Ishida O, Hinoi T, et al. (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.
- Vavvas D, Li X, Avruch J, Zhang XF (1998). "Identification of Nore1 as a potential Ras effector". J. Biol. Chem. 273 (10): 5439–42. doi:10.1074/jbc.273.10.5439. PMID 9488663.
- Kim JH, Lee SD, Han JM, et al. (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.
- Ohta Y, Suzuki N, Nakamura S, et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=26747.
- Wang KL, Roufogalis BD (1999). "Ca2+/calmodulin stimulates GTP binding to the ras-related protein ral-A". J. Biol. Chem. 274 (21): 14525–8. doi:10.1074/jbc.274.21.14525. PMID 10329639.
- Suzuki J, Yamazaki Y, Li G, et al. (2000). "Involvement of Ras and Ral in Chemotactic Migration of Skeletal Myoblasts". Mol. Cell. Biol. 20 (13): 4658–65. doi:10.1128/MCB.20.13.4658-4665.2000. PMC 85875. PMID 10848592. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85875.
- de Bruyn KM, de Rooij J, Wolthuis RM, et al. (2000). "RalGEF2, a pleckstrin homology domain containing guanine nucleotide exchange factor for Ral". J. Biol. Chem. 275 (38): 29761–6. doi:10.1074/jbc.M001160200. PMID 10889189.
- Brymora A, Valova VA, Larsen MR, et al. (2001). "The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene". J. Biol. Chem. 276 (32): 29792–7. doi:10.1074/jbc.C100320200. PMID 11406615.
- Sugihara K, Asano S, Tanaka K, et al. (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.
- Clough RR, Sidhu RS, Bhullar RP (2002). "Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets". J. Biol. Chem. 277 (32): 28972–80. doi:10.1074/jbc.M201504200. PMID 12034722.
- 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Xu L, Frankel P, Jackson D, et al. (2003). "Elevated Phospholipase D Activity in H-Ras- but Not K-Ras-Transformed Cells by the Synergistic Action of RalA and ARF6". Mol. Cell. Biol. 23 (2): 645–54. doi:10.1128/MCB.23.2.645-654.2003. PMC 151535. PMID 12509462. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151535.
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PDB gallery
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1u8y: CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap
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1u8z: Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap
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1u90: Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap
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1uad: Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex
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1zc3: Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA
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1zc4: Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA
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2a78: Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme
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2a9k: Crystal structure of the C3bot-NAD-RalA complex reveals a novel type of action of a bacterial exoenzyme
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2bov: MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE
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