GRB10

Protein-coding gene in the species Homo sapiens


title: "GRB10" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public description: "Protein-coding gene in the species Homo sapiens" topic_path: "uncategorized" source: "https://en.wikipedia.org/wiki/GRB10" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary 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.

Function

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.

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.

Interactions

GRB10 has been shown to interact with

References

References

  1. "Entrez Gene: GRB10 growth factor receptor-bound protein 10".
  2. (February 1997). "Assignment of growth factor receptor-bound protein 10 (GRB10) to human chromosome 7p11.2-p12". Genomics.
  3. (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..
  4. (August 2009). "Reciprocal imprinting of human GRB10 in placental trophoblast and brain: evolutionary conservation of reversed allelic expression". Hum. Mol. Genet..
  5. (January 27, 2011). "Distinct physiological and behavioural functions for parental alleles of imprinted Grb10". Nature.
  6. (August 1998). "The SH2-containing adapter protein GRB10 interacts with BCR-ABL". Oncogene.
  7. (December 1999). "Localization of endogenous Grb10 to the mitochondria and its interaction with the mitochondrial-associated Raf-1 pool". J Biol Chem.
  8. (April 1998). "Interaction of the Grb10 adapter protein with the Raf1 and MEK1 kinases". J Biol Chem.
  9. (February 2002). "Role for the adaptor protein Grb10 in the activation of Akt". Mol Cell Biol.
  10. (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.
  11. (June 2000). "Identification of Grb10 as a direct substrate for members of the Src tyrosine kinase family". Oncogene.
  12. (April 1996). "Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus". J Biol Chem.
  13. (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.
  14. (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.
  15. (May 2003). "The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor". Mol Cell Biol.
  16. (June 1996). "Evidence for the direct interaction of the insulin-like growth factor I receptor with IRS-1, Shc, and Grb10". Mol Endocrinol.
  17. (July 1996). "Grb10: A new substrate of the insulin-like growth factor I receptor". Cancer Res.
  18. (September 1995). "The Ret receptor protein tyrosine kinase associates with the SH2-containing adapter protein Grb10". J Biol Chem.

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