Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH 2 domain‐binding capacity
Year: 2016
Type: article
Abstract: Src family tyrosine kinases (SFKs) are critical players in normal and aberrant biological processes. While phosphorylation importantly regulates SFKs at two known tyrosines, large-scale phosphoproteomics have revealed four additional tyrosines commonly phosphorylated in SFKs. We found these novel tyrosines to be autophosphorylation sites. Mimicking phosphorylation at the C-terminal site to the activation loop decreased Fyn activity. Phosphomimetics and direct phosphorylation at the three SH2 domain sites increased Fyn activity while reducing phosphotyrosine-dependent interactions. While 68% of human SH2 domains exhibit conservation of at least one of these tyrosines, few have been found phosphorylated except when found in cis to a kinase domain.
Source: FEBS Letters
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: bronze
Awards: Vermont Immunobioloigy/ Infectious Diseases Center, G280267960, Center for Neuroscience Excellence, Phosphotyrosine-dependent regulatory mechanisms of mammalian brain development: A large-scale phosphoproteomic and biochemical study., Center for Neuroscience Excellence, Vermont Biomedical Research Network-Vermont INBRE
OpenAlex ID: W2308778564