Grb10 is a dual regulator of receptor tyrosine kinase signaling

Nuzhat N Kabir; Julhash U Kazi

doi:10.1007/s11033-014-3046-4

Grb10 is a dual regulator of receptor tyrosine kinase signaling

Mol Biol Rep. 2014;41(4):1985-92. doi: 10.1007/s11033-014-3046-4. Epub 2014 Jan 14.

Authors

Nuzhat N Kabir¹, Julhash U Kazi

Affiliation

¹ Laboratory of Computational Biochemistry, KN Biomedical Research Institute, Bagura Road, Barisal, Bangladesh.

PMID: 24420853
DOI: 10.1007/s11033-014-3046-4

Abstract

The adaptor protein Grb10 is a close homolog of Grb7 and Grb14. These proteins are characterized by an N-terminal proline-rich region, a Ras-GTPase binding domain, a PH domain, an SH2 domain and a BPS domain in between the PH and SH2 domains. Human Grb10 gene encodes three splice variants. These variants show differences in functionality. Grb10 associates with multiple proteins including tyrosine kinases in a tyrosine phosphorylation dependent or independent manner. Association with multiple proteins allows Grb10 to regulate different signaling pathways resulting in different biological consequences.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Alternative Splicing
Animals
ErbB Receptors / metabolism
GRB10 Adaptor Protein / chemistry
GRB10 Adaptor Protein / genetics
GRB10 Adaptor Protein / metabolism*
Gene Expression
Humans
Protein Interaction Domains and Motifs
Receptor Protein-Tyrosine Kinases / metabolism*
Receptor, Insulin / metabolism
Receptors, Vascular Endothelial Growth Factor / metabolism
Signal Transduction*
src Homology Domains

Substances

GRB10 Adaptor Protein
ErbB Receptors
Receptor Protein-Tyrosine Kinases
Receptor, Insulin
Receptors, Vascular Endothelial Growth Factor