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make fit for, or change to suit a new purpose; "Adapt our native cuisine to the available food resources of the new country" (同)accommodate
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/22 11:21:48」(JST)

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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.^[1]^[2]^[3]^[4]

Function

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 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.^[1]

Animal studies

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.^[5]

Interactions

GRB10 has been shown to interact with

Abl gene,^[6]^[7]
BCR gene,^[6]
C-Raf,^[8]^[9]
c-Kit,^[10]
Insulin receptor,^[7]^[11]^[12]^[13]^[14]
Insulin-like growth factor 1 receptor,^[14]^[15]^[16]^[17]
MAP2K1,^[9] and
RET proto-oncogene.^[18]

References

^ ^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 – New York Times.
^ ^a ^b Bai, R Y; Jahn T; Schrem S; Munzert G; Weidner K M; Wang J Y; Duyster J (Aug 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene 17 (8): 941–8. doi:10.1038/sj.onc.1202024. ISSN 0950-9232. PMID 9747873.
^ ^a ^b Frantz, J D; Giorgetti-Peraldi S; Ottinger E A; Shoelson S E (Jan 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. ISSN 0021-9258. PMID 9006901.
^ Nantel, A; Huber M; Thomas D Y (Dec 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. ISSN 0021-9258. PMID 10585452.
^ ^a ^b Nantel, A; Mohammad-Ali K; Sherk J; Posner B I; Thomas D Y (Apr 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. ISSN 0021-9258. PMID 9553107.
^ Jahn, Thomas; Seipel Petra; Urschel Susanne; Peschel Christian; Duyster Justus (Feb 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. ISSN 0270-7306. PMC 134632. PMID 11809791.
^ Langlais, P; Dong L Q; Hu D; Liu F (Jun 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. ISSN 0950-9232. PMID 10871840.
^ Hansen, H; Svensson U; Zhu J; Laviola L; Giorgino F; Wolf G; Smith R J; Riedel H (Apr 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. ISSN 0021-9258. PMID 8621530.
^ Liu, F; Roth R A (Oct 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. ISSN 0027-8424. PMC 40781. PMID 7479769.
^ ^a ^b He, W; Rose D W; Olefsky J M; Gustafson T A (Mar 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. ISSN 0021-9258. PMID 9506989.
^ Vecchione, Andrea; Marchese Adriano; Henry Pauline; Rotin Daniela; Morrione Andrea (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. ISSN 0270-7306. PMC 153198. PMID 12697834.
^ Dey, B R; Frick K; Lopaczynski W; Nissley S P; Furlanetto R W (Jun 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. ISSN 0888-8809. PMID 8776723.
^ Morrione, A; Valentinis B; Li S; Ooi J Y; Margolis B; Baserga R (Jul 1996). "Grb10: A new substrate of the insulin-like growth factor I receptor". Cancer Res. 56 (14): 3165–7. ISSN 0008-5472. PMID 8764099.
^ Pandey, A; Duan H; Di Fiore P P; Dixit V M (Sep 1995). "The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10". J. Biol. Chem. 270 (37): 21461–3. doi:10.1074/jbc.270.37.21461. ISSN 0021-9258. PMID 7665556.

External links

GRB10 Protein at the US National Library of Medicine Medical Subject Headings (MeSH)

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

UpToDate Contents

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Cyclic Peptides Incorporating Phosphotyrosine Mimetics as Potent and Specific Inhibitors of the Grb7 Breast Cancer Target.

Watson GM, Gunzburg MJ, Ambaye ND, Lucas WA, Traore DA, Kulkarni K, Cergol KM1, Payne RJ1, Panjikar S2, Pero SC3, Perlmutter P, Wilce MC, Wilce JA.
Journal of medicinal chemistry.J Med Chem.2015 Oct 8;58(19):7707-18. doi: 10.1021/acs.jmedchem.5b00609. Epub 2015 Sep 23.
The Grb7 adaptor protein is a therapeutic target for both TNBC and HER2+ breast cancer. A nonphosphorylated cyclic peptide 1 (known as G7-18NATE) inhibits Grb7 via targeting the Grb7-SH2 domain, but requires the presence of phosphate ions for both affinity and specificity. Here we report the discove
PMID 26359549

Aberrant methylation of imprinted genes is associated with negative hormone receptor status in invasive breast cancer.

Barrow TM1,2, Barault L1, Ellsworth RE3, Harris HR1, Binder AM1, Valente AL4, Shriver CD5, Michels KB1,2,6.
International journal of cancer. Journal international du cancer.Int J Cancer.2015 Aug 1;137(3):537-47. doi: 10.1002/ijc.29419. Epub 2015 Jan 21.
Epigenetic regulation of imprinted genes enables monoallelic expression according to parental origin, and its disruption is implicated in many cancers and developmental disorders. The expression of hormone receptors is significant in breast cancer because they are indicators of cancer cell growth ra
PMID 25560175

Tissue-specific regulation and function of Grb10 during growth and neuronal commitment.

Plasschaert RN1, Bartolomei MS2.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2015 Jun 2;112(22):6841-7. doi: 10.1073/pnas.1411254111. Epub 2014 Nov 3.
Growth-factor receptor bound protein 10 (Grb10) is a signal adapter protein encoded by an imprinted gene that has roles in growth control, cellular proliferation, and insulin signaling. Additionally, Grb10 is critical for the normal behavior of the adult mouse. These functions are paralleled by Grb1
PMID 25368187

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★リンクテーブル★

リンク元	「Grb10タンパク質」「増殖因子受容体結合タンパク質10」
関連記事	「adapt」「adaptor protein」「adaptor」

「Grb10タンパク質」

Growth factor receptor-bound protein 10
	PDB rendering based on 1nrv.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1NRV, 3HK0
Identifiers
Symbols	GRB10 ; GRB-IR; Grb-10; IRBP; MEG1; RSS
External IDs	OMIM: 601523 MGI: 103232 HomoloGene: 3882 GeneCards: GRB10 Gene
Gene ontology
Molecular function	• SH3/SH2 adaptor activity; • insulin receptor binding; • protein binding;
Cellular component	• cytoplasm; • cytosol; • plasma membrane;
Biological process	• insulin receptor signaling pathway; • negative regulation of Wnt signaling pathway; • positive regulation of vascular endothelial growth factor receptor signaling pathway; • response to insulin; • negative regulation of phosphorylation; • positive regulation of phosphorylation; • negative regulation of glycogen biosynthetic process; • negative regulation of glucose import; • negative regulation of insulin receptor signaling pathway; • insulin-like growth factor receptor signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;