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GRB7




Growth factor receptor-bound protein 7
PDB rendering based on 1mw4.
Available structures: 1mw4, 1wgr
Identifiers
Symbol(s) GRB7;
External IDs OMIM: 601522 MGI: 102683 Homologene: 3881
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 2886 14786
Ensembl ENSG00000141738 ENSMUSG00000019312
Uniprot Q14451 Q3TH55
Refseq NM_001030002 (mRNA)
NP_001025173 (protein)
NM_010346 (mRNA)
NP_034476 (protein)
Location Chr 17: 35.15 - 35.16 Mb Chr 11: 98.26 - 98.27 Mb
Pubmed search [1] [2]

Growth factor receptor-bound protein 7, also known as GRB7, is a human gene.[1]

The product of this gene belongs to a small family of adapter proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with epidermal growth factor receptor (EGFR) and ephrin receptors. The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase (FAK). Alternative splicing results in multiple transcript variants encoding different isoforms, although the full-length natures of only two of the variants have been determined to date.[1]

GRB7 is an SH2-domain adaptor protein that binds to Receptor-tyrosine kinases and provides the intra-cellular direct link to the Ras proto-oncogene. Human GRB7 is located on the long arm of chromosome 17, next to the ERBB2 (alias her2/neu) proto-oncogene.

These two genes are commonly co-amplified (present in excess copies) in breast cancers. GRB7, thought to be involved in migration[citation needed], is well known to be over-expressed in testicular germ cell tumors, esophagous cancers, and gastric cancers.

References

  1. ^ a b Entrez Gene: GRB7 growth factor receptor-bound protein 7.

Further reading

  • Han DC, Shen TL, Guan JL (2001). "The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions.". Oncogene 20 (44): 6315-21. doi:10.1038/sj.onc.1204775. PMID 11607834.
  • Margolis B, Silvennoinen O, Comoglio F, et al. (1992). "High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains.". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 8894-8. PMID 1409582.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
  • Pandey A, Liu X, Dixon JE, et al. (1996). "Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7.". J. Biol. Chem. 271 (18): 10607-10. PMID 8631863.
  • Yokote K, Margolis B, Heldin CH, Claesson-Welsh L (1997). "Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors.". J. Biol. Chem. 271 (48): 30942-9. PMID 8940081.
  • Tanaka S, Mori M, Akiyoshi T, et al. (1997). "Coexpression of Grb7 with epidermal growth factor receptor or Her2/erbB2 in human advanced esophageal carcinoma.". Cancer Res. 57 (1): 28-31. PMID 8988034.
  • Janes PW, Lackmann M, Church WB, et al. (1997). "Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7.". J. Biol. Chem. 272 (13): 8490-7. PMID 9079677.
  • Kishi T, Sasaki H, Akiyama N, et al. (1997). "Molecular cloning of human GRB-7 co-amplified with CAB1 and c-ERBB-2 in primary gastric cancer.". Biochem. Biophys. Res. Commun. 232 (1): 5-9. doi:10.1006/bbrc.1997.6218. PMID 9125150.
  • Dong LQ, Du H, Porter SG, et al. (1997). "Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma.". J. Biol. Chem. 272 (46): 29104-12. PMID 9360986.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
  • Fiddes RJ, Campbell DH, Janes PW, et al. (1998). "Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3.". J. Biol. Chem. 273 (13): 7717-24. PMID 9516479.
  • Tanaka S, Mori M, Akiyoshi T, et al. (1998). "A novel variant of human Grb7 is associated with invasive esophageal carcinoma.". J. Clin. Invest. 102 (4): 821-7. PMID 9710451.
  • Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L (1999). "Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor.". Biochem. J. 341 ( Pt 1): 211-6. PMID 10377264.
  • Han DC, Guan JL (1999). "Association of focal adhesion kinase with Grb7 and its role in cell migration.". J. Biol. Chem. 274 (34): 24425-30. PMID 10446223.
  • Jones N, Master Z, Jones J, et al. (1999). "Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration.". J. Biol. Chem. 274 (43): 30896-905. PMID 10521483.
  • Vayssière B, Zalcman G, Mahé Y, et al. (2000). "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family.". FEBS Lett. 467 (1): 91-6. PMID 10664463.
  • Kasus-Jacobi A, Béréziat V, Perdereau D, et al. (2000). "Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2.". Oncogene 19 (16): 2052-9. doi:10.1038/sj.onc.1203469. PMID 10803466.
  • Han DC, Shen TL, Guan JL (2000). "Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration.". J. Biol. Chem. 275 (37): 28911-7. doi:10.1074/jbc.M001997200. PMID 10893408.
  • Lee H, Volonte D, Galbiati F, et al. (2001). "Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: identification of a c-Src/Cav-1/Grb7 signaling cassette.". Mol. Endocrinol. 14 (11): 1750-75. PMID 11075810.
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "GRB7". A list of authors is available in Wikipedia.
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