Protein-coding gene in the species Homo sapiens
Growth factor receptor-bound protein 10 also known as insulin receptor-binding protein Grb-IR is a protein that in humans is encoded by the GRB10 gene .[ 5] [ 6] [ 7] [ 8]
The product of this gene belongs to a small family of adaptor 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 insulin receptors and insulin-like growth-factor receptors (e.g., IGF1R and IGF2R ). Overexpression of some isoforms of the encoded protein inhibits tyrosine kinase activity and results in growth suppression. This gene is imprinted in a highly isoform- and tissue-specific manner. Alternatively spliced transcript variants encoding different isoforms have been identified.[ 5]
Mice whose paternally inherited Grb10 gene is inactivated are more aggressive while those whose maternally inherited allele is inactivated exhibit foetal overgrowth and are significantly bigger than wild-type litter-mates.[ 9]
GRB10 has been shown to interact with
^ a b c GRCh38: Ensembl release 89: ENSG00000106070 – Ensembl , May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020176 – Ensembl , May 2017
^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ a b "Entrez Gene: GRB10 growth factor receptor-bound protein 10" .
^ Jerome CA, Scherer SW, Tsui LC, Gietz RD, Triggs-Raine B (February 1997). "Assignment of growth factor receptor-bound protein 10 (GRB10) to human chromosome 7p11.2-p12". Genomics . 40 (1): 215–6. doi :10.1006/geno.1996.4535 . PMID 9070953 .
^ Dong LQ, Du H, Porter SG, Kolakowski LF, Lee AV, Mandarino LJ, Fan J, Yee D, Liu F, Mandarino J (November 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. doi :10.1074/jbc.272.46.29104 . PMID 9360986 .
^ Monk D, Arnaud P, Frost J, Hills FA, Stanier P, Feil R, Moore GE (August 2009). "Reciprocal imprinting of human GRB10 in placental trophoblast and brain: evolutionary conservation of reversed allelic expression" . Hum. Mol. Genet . 18 (16): 3066–74. doi :10.1093/hmg/ddp248 . PMID 19487367 .
^ Garfield AS, Cowley M, Smith FM, Moorwood K, Stewart-Cox JE, Gilroy K, Baker S, Xia J, Dalley JW, Hurst LD, Wilkinson LS, Isles AR, Ward A (2011). "Distinct physiological and behavioural functions for parental alleles of imprinted Grb10" . Nature . 469 (7331): 534–538. Bibcode :2011Natur.469..534G . doi :10.1038/nature09651 . PMC 3031026 . PMID 21270893 . *Lay summary in: Bhanoo SN (January 27, 2011). "Altering a Mouse Gene Turns Up Aggression, Study Says" . New York Times .
^ a b Bai RY, Jahn T, Schrem S, Munzert G, Weidner KM, Wang JY, Duyster J (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL" . Oncogene . 17 (8): 941–8. doi :10.1038/sj.onc.1202024 . PMID 9747873 .
^ a b Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE (January 1997). "Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains" . J Biol Chem . 272 (5): 2659–67. doi :10.1074/jbc.272.5.2659 . PMID 9006901 .
^ Nantel A, Huber M, Thomas DY (December 1999). "Localization of endogenous Grb10 to the mitochondria and its interaction with the mitochondrial-associated Raf-1 pool" . J Biol Chem . 274 (50): 35719–24. doi :10.1074/jbc.274.50.35719 . PMID 10585452 .
^ a b Nantel A, Mohammad-Ali K, Sherk J, Posner BI, Thomas DY (April 1998). "Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases" . J Biol Chem . 273 (17): 10475–84. doi :10.1074/jbc.273.17.10475 . PMID 9553107 .
^ Jahn T, Seipel P, Urschel S, Peschel C, Duyster J (February 2002). "Role for the adaptor protein Grb10 in the activation of Akt" . Mol Cell Biol . 22 (4): 979–91. doi :10.1128/MCB.22.4.979-991.2002 . PMC 134632 . PMID 11809791 .
^ Langlais P, Dong LQ, Hu D, Liu F (June 2000). "Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family" . Oncogene . 19 (25): 2895–903. doi :10.1038/sj.onc.1203616 . PMID 10871840 .
^ Hansen H, Svensson U, Zhu J, Laviola L, Giorgino F, Wolf G, Smith RJ, Riedel H (April 1996). "Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus" . J Biol Chem . 271 (15): 8882–6. doi :10.1074/jbc.271.15.8882 . PMID 8621530 .
^ Liu F, Roth RA (October 1995). "Grb-IR: a SH2-domain-containing protein that binds to the insulin receptor and inhibits its function" . Proc Natl Acad Sci U S A . 92 (22): 10287–91. Bibcode :1995PNAS...9210287L . doi :10.1073/pnas.92.22.10287 . PMC 40781 . PMID 7479769 .
^ a b He W, Rose DW, Olefsky JM, Gustafson TA (March 1998). "Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains" . J Biol Chem . 273 (12): 6860–7. doi :10.1074/jbc.273.12.6860 . PMID 9506989 .
^ Vecchione A, Marchese A, Henry P, Rotin D, Morrione A (May 2003). "The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor" . Mol Cell Biol . 23 (9): 3363–72. doi :10.1128/MCB.23.9.3363-3372.2003 . PMC 153198 . PMID 12697834 .
^ Dey BR, Frick K, Lopaczynski W, Nissley SP, Furlanetto RW (June 1996). "Evidence for the direct interaction of the insulin-like growth factor I receptor with IRS-1, Shc, and Grb10" . Mol Endocrinol . 10 (6): 631–41. doi :10.1210/mend.10.6.8776723 . PMID 8776723 .
^ Morrione A, Valentinis B, Li S, Ooi JY, Margolis B, Baserga R (July 1996). "Grb10: A new substrate of the insulin-like growth factor I receptor". Cancer Res . 56 (14): 3165–7. PMID 8764099 .
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This article incorporates text from the United States National Library of Medicine , which is in the public domain .