Biology:SOS1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Son of sevenless homolog 1 is a protein that in humans is encoded by the SOS1 gene.[1][2]

Function

SOS1 is a guanine nucleotide exchange factor (GEF) which interacts with RAS proteins to phosphorylate GDP into GTP, or from an inactive state to an active state to signal cell proliferation. 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.[3]

Clinical significance

Recent studies also show that mutations in Sos1 can cause Noonan syndrome[4] and hereditary gingival fibromatosis type 1.[5] Noonan syndrome has also been shown to be caused by mutations in KRAS and PTPN11 genes.[6] activators of the MAP kinase pathway.

Interactions

SOS1 has been shown to interact with:


See also

References

  1. ↑ "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. February 1994. doi:10.1006/geno.1993.1421. PMID 8276400. 
  2. ↑ "Refinement of the locus for autosomal dominant hereditary gingival fibromatosis (GINGF) to a 3.8-cM region on 2p21". Genomics 68 (3): 247–52. November 2000. doi:10.1006/geno.2000.6285. PMID 10995566. 
  3. ↑ "Entrez Gene: SOS1 son of sevenless homolog 1 (Drosophila)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6654. 
  4. ↑ "Germline gain-of-function mutations in SOS1 cause Noonan syndrome". Nat. Genet. 39 (1): 70–4. January 2007. doi:10.1038/ng1926. PMID 17143285. 
  5. ↑ "A mutation in the SOS1 gene causes hereditary gingival fibromatosis type 1". Am. J. Hum. Genet. 70 (4): 943–54. April 2002. doi:10.1086/339689. PMID 11868160. 
  6. ↑ "Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome". Nat. Genet. 29 (4): 465–8. December 2001. doi:10.1038/ng772. PMID 11704759. 
  7. ↑ 7.0 7.1 "EPS8 and E3B1 transduce signals from Ras to Rac". Nature 401 (6750): 290–3. September 1999. doi:10.1038/45822. PMID 10499589. Bibcode: 1999Natur.401..290S. 
  8. ↑ 8.0 8.1 "Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway". EMBO J. 13 (4): 764–73. February 1994. doi:10.1002/j.1460-2075.1994.tb06319.x. PMID 8112292. 
  9. ↑ "Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS". Mol. Cell. Biol. 15 (2): 835–42. February 1995. doi:10.1128/MCB.15.2.835. PMID 7529874. 
  10. ↑ 10.0 10.1 10.2 "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. October 1996. doi:10.1074/jbc.271.41.25533. PMID 8810325. 
  11. ↑ "The eps8 family of proteins links growth factor stimulation to actin reorganization generating functional redundancy in the Ras/Rac pathway". Mol. Biol. Cell 15 (1): 91–8. January 2004. doi:10.1091/mbc.E03-06-0427. PMID 14565974. 
  12. ↑ 12.0 12.1 "A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells". J. Biol. Chem. 269 (12): 9019–23. March 1994. doi:10.1016/S0021-9258(17)37070-9. PMID 7510700. 
  13. ↑ 13.0 13.1 "The Sos1 and Sos2 Ras-specific exchange factors: differences in placental expression and signaling properties". EMBO J. 19 (4): 642–54. February 2000. doi:10.1093/emboj/19.4.642. PMID 10675333. 
  14. ↑ "N terminus of Sos1 Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains". Mol. Cell. Biol. 18 (2): 771–8. February 1998. doi:10.1128/mcb.18.2.771. PMID 9447973. 
  15. ↑ 15.0 15.1 "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl". Proc. Natl. Acad. Sci. U.S.A. 99 (10): 6684–9. May 2002. doi:10.1073/pnas.052138899. PMID 11997436. Bibcode: 2002PNAS...99.6684W. 
  16. ↑ 16.0 16.1 "Discoidin domain receptor 1 (DDR1) signaling in PC12 cells: activation of juxtamembrane domains in PDGFR/DDR/TrkA chimeric receptors". FASEB J. 14 (7): 973–81. May 2000. doi:10.1096/fasebj.14.7.973. PMID 10783152. 
  17. ↑ "A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway". Cell 89 (5): 693–702. May 1997. doi:10.1016/s0092-8674(00)80252-4. PMID 9182757. 
  18. ↑ 18.0 18.1 18.2 "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. October 1997. doi:10.1006/bbrc.1997.7480. PMID 9344843. 
  19. ↑ 19.0 19.1 "Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein". Cancer Res. 55 (18): 4000–3. September 1995. PMID 7664271. 
  20. ↑ "A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling". Nat. Biotechnol. 21 (3): 315–8. March 2003. doi:10.1038/nbt790. PMID 12577067. 
  21. ↑ "Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc". Oncogene 17 (24): 3073–82. Dec 1998. doi:10.1038/sj.onc.1202337. PMID 9872323. 
  22. ↑ "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drug". Oncogene 21 (13): 2037–50. March 2002. doi:10.1038/sj.onc.1205271. PMID 11960376. 
  23. ↑ "Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking". Blood 88 (2): 522–30. July 1996. doi:10.1182/blood.V88.2.522.bloodjournal882522. PMID 8695800. 
  24. ↑ "Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling". Nature 363 (6424): 85–8. May 1993. doi:10.1038/363085a0. PMID 8479541. Bibcode: 1993Natur.363...85L. 
  25. ↑ "SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases". J. Biol. Chem. 269 (19): 14081–7. May 1994. doi:10.1016/S0021-9258(17)36757-1. PMID 8188688. 
  26. ↑ "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Mol. Endocrinol. 13 (5): 692–704. May 1999. doi:10.1210/mend.13.5.0280. PMID 10319320. 
  27. ↑ "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. August 1995. doi:10.1074/jbc.270.31.18428. PMID 7629168. 
  28. ↑ 28.0 28.1 "The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain". EMBO J. 19 (6): 1263–71. March 2000. doi:10.1093/emboj/19.6.1263. PMID 10716926. 
  29. ↑ "Role of Src in the modulation of multiple adaptor proteins in FcalphaRI oxidant signaling". Blood 94 (6): 2112–20. September 1999. doi:10.1182/blood.V94.6.2112. PMID 10477741. 
  30. ↑ "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways". Mol. Cell. Biol. 19 (5): 3798–807. May 1999. doi:10.1128/MCB.19.5.3798. PMID 10207103. 
  31. ↑ 31.0 31.1 "High affinity IgG receptor activation of Src family kinases is required for modulation of the Shc-Grb2-Sos complex and the downstream activation of the nicotinamide adenine dinucleotide phosphate (reduced) oxidase". J. Immunol. 163 (11): 6023–34. Dec 1999. doi:10.4049/jimmunol.163.11.6023. PMID 10570290. 
  32. ↑ "Differential effect of the inhibition of Grb2-SH3 interactions in platelet activation induced by thrombin and by Fc receptor engagement". Biochem. J. 363 (Pt 3): 717–25. May 2002. doi:10.1042/0264-6021:3630717. PMID 11964172. 
  33. ↑ "Multiple Grb2-protein complexes in human cancer cells". Int. J. Cancer 70 (2): 208–13. January 1997. doi:10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e. PMID 9009162. 
  34. ↑ "Point mutation in the fibroblast growth factor receptor eliminates phosphatidylinositol hydrolysis without affecting neuronal differentiation of PC12 cells". J. Biol. Chem. 269 (20): 14419–23. May 1994. doi:10.1016/S0021-9258(17)36639-5. PMID 7514169. 
  35. ↑ "Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS". Cell 112 (5): 685–95. March 2003. doi:10.1016/s0092-8674(03)00149-1. PMID 12628188. 
  36. ↑ "The structural basis of the activation of Ras by Sos". Nature 394 (6691): 337–43. July 1998. doi:10.1038/28548. PMID 9690470. Bibcode: 1998Natur.394..337B. 
  37. ↑ "Transgenic MUC1 interacts with epidermal growth factor receptor and correlates with mitogen-activated protein kinase activation in the mouse mammary gland". J. Biol. Chem. 276 (16): 13057–64. April 2001. doi:10.1074/jbc.M011248200. PMID 11278868. 
  38. ↑ "Characterization of interactions of Nck with Sos and dynamin". Cell. Signal. 11 (1): 25–9. January 1999. doi:10.1016/s0898-6568(98)00027-8. PMID 10206341. 
  39. ↑ "Binding of NCK to SOS and activation of ras-dependent gene expression". Mol. Cell. Biol. 15 (3): 1169–74. March 1995. doi:10.1128/MCB.15.3.1169. PMID 7862111. 
  40. ↑ "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. 274 (9): 5542–9. February 1999. doi:10.1074/jbc.274.9.5542. PMID 10026169. 
  41. ↑ "Direct interaction of SOS1 Ras exchange protein with the SH3 domain of phospholipase C-gamma1". Biochemistry 39 (29): 8674–82. July 2000. doi:10.1021/bi992558t. PMID 10913276. 
  42. ↑ "Engagement of the T lymphocyte antigen receptor regulates association of son-of-sevenless homologues with the SH3 domain of phospholipase Cgamma1". Eur. J. Immunol. 30 (8): 2378–87. August 2000. doi:10.1002/1521-4141(2000)30:8<2378::AID-IMMU2378>3.0.CO;2-E. PMID 10940929. 
  43. ↑ "Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation". Mol. Cell. Biol. 18 (7): 3966–73. July 1998. doi:10.1128/MCB.18.7.3966. PMID 9632781. 
  44. ↑ "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes". Biochem. Biophys. Res. Commun. 278 (1): 167–74. November 2000. doi:10.1006/bbrc.2000.3760. PMID 11071869. https://zenodo.org/record/1229524. 

Further reading

External links

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




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