Novel autophosphorylation sites of Src family kinases regulate kinase activity and SH2 domain-binding capacity.
FEBS Lett
; 590(8): 1042-52, 2016 04.
Article
em En
| MEDLINE
| ID: mdl-27001024
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.
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MEDLINE
Assunto principal:
Quinases da Família src
/
Domínios de Homologia de src
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article