Grb2 binding induces phosphorylation-independent activation of Shp2

• Published in: Communications biology Vol. 4; no. 1; p. 437
• Main Authors: Lin, Chi-Chuan, Wieteska, Lukasz, Suen, Kin Man, Kalverda, Arnout P., Ahmed, Zamal, Ladbury, John E.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01.04.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 13; 13/1; 14; 14/33; 14/35; 631/45/173; 631/80/86/2368; 82/29; 82/6; 82/80; 9/10; 96/10; 96/106; 96/95; Biology; Biomedical and Life Sciences; Breast cancer; Cancer; Cytoplasm; Enzyme Activation; GRB2 Adaptor Protein - genetics; GRB2 Adaptor Protein - metabolism; Grb2 protein; Hyperactivity; Intracellular signalling; Kinases; Life Sciences; MAP kinase; Phosphatase; Phosphorylation; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - genetics; Protein Tyrosine Phosphatase, Non-Receptor Type 11 - metabolism; Protein-tyrosine kinase receptors; Protein-tyrosine-phosphatase; Proteins; Signal Transduction

The regulation of phosphatase activity is fundamental to the control of intracellular signalling and in particular the tyrosine kinase-mediated mitogen-activated protein kinase (MAPK) pathway. Shp2 is a ubiquitously expressed protein tyrosine phosphatase and its kinase-induced hyperactivity is assoc...