SOS1

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Son of sevenless homolog 1 (Drosophila)
File:PBB Protein SOS1 image.jpg
PDB rendering based on 1awe.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SOS1 ; GF1; HGF; GGF1; GINGF; NS4
External IDs Template:OMIM5 Template:MGI HomoloGene4117
RNA expression pattern
File:PBB GE SOS1 212777 at tn.png
File:PBB GE SOS1 212780 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Son of sevenless homolog 1 (Drosophila), also known as SOS1, is a human gene. RAS genes (e.g., MIM 190020) encode membrane-bound guanine nucleotide-binding proteins that function in the transduction of signals that control cell growth and differentiation. Binding of GTP activates RAS proteins, and subsequent hydrolysis of the bound GTP to GDP and phosphate inactivates signaling by these proteins. GTP binding can be catalyzed by guanine nucleotide exchange factors for RAS, and GTP hydrolysis can be accelerated by GTPase-activating proteins (GAPs). The first exchange factor to be identified for RAS was the S. cerevisiae CDC25 gene product. Genetic analysis indicated that CDC25 is essential for activation of RAS proteins. In Drosophila, the protein encoded by the 'son of sevenless' gene (Sos) contains a domain that shows sequence similarity with the catalytic domain of CDC25. Sos may act as a positive regulator of RAS by promoting guanine nucleotide exchange.[supplied by OMIM][1] Recent studies also show that mutations in Sos1 can cause Noonan syndrome.

See also

References

  1. "Entrez Gene: SOS1 son of sevenless homolog 1 (Drosophila)".

External links

Further reading

  • Lioubin MN, Myles GM, Carlberg K; et al. (1994). "Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells". Mol. Cell. Biol. 14 (9): 5682–91. PMID 7520523.
  • Nel AE, Gupta S, Lee L; et al. (1995). "Ligation of the T-cell antigen receptor (TCR) induces association of hSos1, ZAP-70, phospholipase C-gamma 1, and other phosphoproteins with Grb2 and the zeta-chain of the TCR". J. Biol. Chem. 270 (31): 18428–36. PMID 7629168.
  • Pandey P, Kharbanda S, Kufe D (1995). "Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein". Cancer Res. 55 (18): 4000–3. PMID 7664271.
  • Hu Q, Milfay D, Williams LT (1995). "Binding of NCK to SOS and activation of ras-dependent gene expression". Mol. Cell. Biol. 15 (3): 1169–74. PMID 7862111.
  • Puil L, Liu J, Gish G; et al. (1994). "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. PMID 8112292.
  • Webb GC, Jenkins NA, Largaespada DA; et al. (1994). "Mammalian homologues of the Drosophila Son of sevenless gene map to murine chromosomes 17 and 12 and to human chromosomes 2 and 14, respectively". Genomics. 18 (1): 14–9. doi:10.1006/geno.1993.1421. PMID 8276400.
  • Li N, Batzer A, Daly R; et al. (1993). "Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling". Nature. 363 (6424): 85–8. doi:10.1038/363085a0. PMID 8479541.
  • Chardin P, Camonis JH, Gale NW; et al. (1993). "Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2". Science. 260 (5112): 1338–43. PMID 8493579.
  • Sadoshima J, Izumo S (1996). "The heterotrimeric G q protein-coupled angiotensin II receptor activates p21 ras via the tyrosine kinase-Shc-Grb2-Sos pathway in cardiac myocytes". EMBO J. 15 (4): 775–87. PMID 8631299.
  • Feng GS, Ouyang YB, Hu DP; et al. (1996). "Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway". J. Biol. Chem. 271 (21): 12129–32. PMID 8647802.
  • Okada S, Pessin JE (1996). "Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor". J. Biol. Chem. 271 (41): 25533–8. PMID 8810325.
  • Corbalan-Garcia S, Yang SS, Degenhardt KR, Bar-Sagi D (1996). "Identification of the mitogen-activated protein kinase phosphorylation sites on human Sos1 that regulate interaction with Grb2". Mol. Cell. Biol. 16 (10): 5674–82. PMID 8816480.
  • Sattler M, Salgia R, Shrikhande G; et al. (1997). "Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1)". J. Biol. Chem. 272 (22): 14320–6. PMID 9162067.
  • Leprince C, Romero F, Cussac D; et al. (1997). "A new member of the amphiphysin family connecting endocytosis and signal transduction pathways". J. Biol. Chem. 272 (24): 15101–5. PMID 9182529.
  • Kouhara H, Hadari YR, Spivak-Kroizman T; et al. (1997). "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway". Cell. 89 (5): 693–702. PMID 9182757.
  • Chin H, Saito T, Arai A; et al. (1997). "Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells". Biochem. Biophys. Res. Commun. 239 (2): 412–7. doi:10.1006/bbrc.1997.7480. PMID 9344843.
  • Zheng J, Chen RH, Corblan-Garcia S; et al. (1997). "The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains". J. Biol. Chem. 272 (48): 30340–4. PMID 9374522.
  • Li S, Kim M, Hu YL; et al. (1997). "Fluid shear stress activation of focal adhesion kinase. Linking to mitogen-activated protein kinases". J. Biol. Chem. 272 (48): 30455–62. PMID 9374537.
  • Qian X, Vass WC, Papageorge AG; et al. (1998). "N terminus of Sos1 Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains". Mol. Cell. Biol. 18 (2): 771–8. PMID 9447973.
  • Curto M, Frankel P, Carrero A, Foster DA (1998). "Novel recruitment of Shc, Grb2, and Sos by fibroblast growth factor receptor-1 in v-Src-transformed cells". Biochem. Biophys. Res. Commun. 243 (2): 555–60. doi:10.1006/bbrc.1997.7982. PMID 9480847.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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