RALGDS

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1RAX, 2B3A, 2RGF, 3KH0

Identifiers

Aliases

RALGDS, RGDS, RGF, RalGEF, ral guanine nucleotide dissociation stimulator

External IDs

MGI: 107485 HomoloGene: 4562 GeneCards: RALGDS

Gene ontology
Molecular function	• protein binding • guanyl-nucleotide exchange factor activity • GTPase regulator activity
Cellular component	• cytosol • brush border • cytoplasm • nucleus
Biological process	• small GTPase mediated signal transduction • positive regulation of GTPase activity • Ras protein signal transduction • signal transduction • regulation of catalytic activity
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5900


19730

Ensembl


ENSG00000160271


ENSMUSG00000026821

UniProt


Q12967


Q03385

RefSeq (mRNA)


NM_006266 NM_001042368 NM_001271774 NM_001271775 NM_001271776


NM_001145834 NM_001145835 NM_001145836 NM_009058

RefSeq (protein)


NP_001035827.1 NP_001258703.1 NP_001258704.1 NP_001258705.1 NP_006257.1


NP_033084.2

Location (UCSC)

Chr 9: 133.1 – 133.15 Mb

Chr 2: 28.51 – 28.55 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Ral guanine nucleotide dissociation stimulator is a protein that in humans is encoded by the RALGDS gene.^[3]^[4]

Interactions

RALGDS has been shown to interact with:

Arrestin beta 1,^[5]
Arrestin beta 2,^[5]
HRAS,^[3]^[6]^[7]^[8]^[9]^[10]^[11]^[12]
KRAS,^[6]^[8]
MRAS,^[13]^[14]
RAP1A,^[7]^[15]
RAP2A,^[15]
RAPGEF2,^[6] and
RRAS.^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Hofer F, Fields S, Schneider C, Martin GS (December 1994). "Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator". Proc Natl Acad Sci U S A. 91 (23): 11089–93. doi:10.1073/pnas.91.23.11089. PMC 45172. PMID 7972015.
↑ "Entrez Gene: RALGDS ral guanine nucleotide dissociation stimulator".
1 2 Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nat. Cell Biol. 4 (8): 547–55. doi:10.1038/ncb821. PMID 12105416.
1 2 3 4 Spaargaren M, Bischoff JR (December 1994). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
1 2 Boettner B, Govek EE, Cross J, Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
1 2 Li W, Han M, Guan KL (April 2000). "The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf". Genes Dev. 14 (8): 895–900. PMC 316541. PMID 10783161.
↑ Mitin NY, Ramocki MB, Zullo AJ, Der CJ, Konieczny SF, Taparowsky EJ (May 2004). "Identification and characterization of rain, a novel Ras-interacting protein with a unique subcellular localization". J. Biol. Chem. 279 (21): 22353–61. doi:10.1074/jbc.M312867200. PMID 15031288.
↑ Miller MJ, Prigent S, Kupperman E, Rioux L, Park SH, Feramisco JR, White MA, Rutkowski JL, Meinkoth JL (February 1997). "RalGDS functions in Ras- and cAMP-mediated growth stimulation". J. Biol. Chem. 272 (9): 5600–5. doi:10.1074/jbc.272.9.5600. PMID 9038168.
↑ Rodriguez-Viciana P, Warne PH, Khwaja A, Marte BM, Pappin D, Das P, Waterfield MD, Ridley A, Downward J (May 1997). "Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras". Cell. 89 (3): 457–67. doi:10.1016/s0092-8674(00)80226-3. PMID 9150145.
↑ Stang S, Bottorff D, Stone JC (June 1997). "Interaction of activated Ras with Raf-1 alone may be sufficient for transformation of rat2 cells". Mol. Cell. Biol. 17 (6): 3047–55. PMC 232157. PMID 9154803.
↑ Kimmelman A, Tolkacheva T, Lorenzi MV, Osada M, Chan AM (November 1997). "Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution". Oncogene. 15 (22): 2675–85. doi:10.1038/sj.onc.1201674. PMID 9400994.
↑ Ehrhardt GR, Leslie KB, Lee F, Wieler JS, Schrader JW (October 1999). "M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line". Blood. 94 (7): 2433–44. PMID 10498616.
1 2 Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (March 1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.

Spaargaren M, Bischoff JR (1995). "Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap". Proc. Natl. Acad. Sci. U.S.A. 91 (26): 12609–13. doi:10.1073/pnas.91.26.12609. PMC 45488. PMID 7809086.
Albright CF, Giddings BW, Liu J, Vito M, Weinberg RA (1993). "Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase". EMBO J. 12 (1): 339–47. PMC 413211. PMID 8094051.
Urano T, Emkey R, Feig LA (1996). "Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation". EMBO J. 15 (4): 810–6. PMC 450279. PMID 8631302.
Miller MJ, Prigent S, Kupperman E, Rioux L, Park SH, Feramisco JR, White MA, Rutkowski JL, Meinkoth JL (1997). "RalGDS functions in Ras- and cAMP-mediated growth stimulation". J. Biol. Chem. 272 (9): 5600–5. doi:10.1074/jbc.272.9.5600. PMID 9038168.
Fukunaga R, Hunter T (1997). "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates". EMBO J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMC 1169795. PMID 9155018.
Geyer M, Herrmann C, Wohlgemuth S, Wittinghofer A, Kalbitzer HR (1997). "Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling". Nat. Struct. Biol. 4 (9): 694–9. doi:10.1038/nsb0997-694. PMID 9302994.
Humphrey D, Kwiatkowska J, Henske EP, Haines JL, Halley D, van Slegtenhorst M, Kwiatkowski DJ (1997). "Cloning and evaluation of RALGDS as a candidate for the tuberous sclerosis gene TSC1". Ann. Hum. Genet. 61 (Pt 4): 299–305. doi:10.1046/j.1469-1809.1997.6140299.x. PMID 9365783.
Kimmelman A, Tolkacheva T, Lorenzi MV, Osada M, Chan AM (1998). "Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution". Oncogene. 15 (22): 2675–85. doi:10.1038/sj.onc.1201674. PMID 9400994.
Shirouzu M, Morinaka K, Koyama S, Hu CD, Hori-Tamura N, Okada T, Kariya K, Kataoka T, Kikuchi A, Yokoyama S (1998). "Interactions of the amino acid residue at position 31 of the c-Ha-Ras protein with Raf-1 and RalGDS". J. Biol. Chem. 273 (13): 7737–42. doi:10.1074/jbc.273.13.7737. PMID 9516482.
Okada S, Matsuda M, Anafi M, Pawson T, Pessin JE (1998). "Insulin regulates the dynamic balance between Ras and Rap1 signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes". EMBO J. 17 (9): 2554–65. doi:10.1093/emboj/17.9.2554. PMC 1170597. PMID 9564038.
Nancy V, Wolthuis RM, de Tand MF, Janoueix-Lerosey I, Bos JL, de Gunzburg J (1999). "Identification and characterization of potential effector molecules of the Ras-related GTPase Rap2". J. Biol. Chem. 274 (13): 8737–45. doi:10.1074/jbc.274.13.8737. PMID 10085114.
Ehrhardt GR, Leslie KB, Lee F, Wieler JS, Schrader JW (1999). "M-Ras, a widely expressed 29-kD homologue of p21 Ras: expression of a constitutively active mutant results in factor-independent growth of an interleukin-3-dependent cell line". Blood. 94 (7): 2433–44. PMID 10498616.
Shao H, Kadono-Okuda K, Finlin BS, Andres DA (1999). "Biochemical characterization of the Ras-related GTPases Rit and Rin". Arch. Biochem. Biophys. 371 (2): 207–19. doi:10.1006/abbi.1999.1448. PMID 10545207.
Zheng Q, Yu L, Zhao Y, Sun X, Dai F, Hu P, Fu Q, Geng Z (2000). "[Refined chromosome assignment of human novel H-RalGDS gene on chromosome 9q34.1 by using radiation hybrid genebridge 4 panel]". Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 17 (1): 1–5. PMID 10653898.
Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
Zheng Q, Yu L, Zhao Y, Zhang H, Fu Q, Mao N, Hu P, Geng Z, Zhao S (2001). "Structure characterization of human RalGDS gene, and the identification of its novel variant". Mol. Biol. Rep. 27 (4): 209–16. doi:10.1023/A:1011043122220. PMID 11455956.
Murphy GA, Graham SM, Morita S, Reks SE, Rogers-Graham K, Vojtek A, Kelley GG, Der CJ (2002). "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation". J. Biol. Chem. 277 (12): 9966–75. doi:10.1074/jbc.M109059200. PMID 11788587.
Ramírez de Molina A, Penalva V, Lucas L, Lacal JC (2002). "Regulation of choline kinase activity by Ras proteins involves Ral-GDS and PI3K". Oncogene. 21 (6): 937–46. doi:10.1038/sj.onc.1205144. PMID 11840339.
Tian X, Rusanescu G, Hou W, Schaffhausen B, Feig LA (2002). "PDK1 mediates growth factor-induced Ral-GEF activation by a kinase-independent mechanism". EMBO J. 21 (6): 1327–38. doi:10.1093/emboj/21.6.1327. PMC 125928. PMID 11889038.

PDB gallery

1lfd: CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS

1lxd: CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN

1rax: RA-DOMAIN OF RAL GUANOSINE-NUCLEOTIDE DISSOCIATION STIMULATOR

2b3a: Solution structure of the Ras-binding domain of the Ral Guanosine Dissociation Stimulator

2rgf: RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10 STRUCTURES

This article is issued from Wikipedia - version of the 5/20/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

RALGDS

Interactions

References

Further reading