Suppression of EGFR autophosphorylation by FKBP12
S Mathea, S Li, A Schierhorn, G Jahreis… - Biochemistry, 2011 - ACS Publications
S Mathea, S Li, A Schierhorn, G Jahreis, C Schiene-Fischer
Biochemistry, 2011•ACS PublicationsFK506 binding proteins (FKBPs) represent a subfamily of peptidyl prolyl cis/trans
isomerases that can control receptor-mediated intracellular signaling. The prototypic PPIase
FKBP12 functionally interacts with EGFR. FKBP12 was shown to inhibit EGF-induced EGFR
autophosphorylation with all internal phosphorylation sites equally affected. The inhibition of
EGFR catalytic activity is conducted by targeting the EGFR kinase domain. The change of
intracellular FKBP12 levels resulted in a change of EGFR autophosphorylation level …
isomerases that can control receptor-mediated intracellular signaling. The prototypic PPIase
FKBP12 functionally interacts with EGFR. FKBP12 was shown to inhibit EGF-induced EGFR
autophosphorylation with all internal phosphorylation sites equally affected. The inhibition of
EGFR catalytic activity is conducted by targeting the EGFR kinase domain. The change of
intracellular FKBP12 levels resulted in a change of EGFR autophosphorylation level …
FK506 binding proteins (FKBPs) represent a subfamily of peptidyl prolyl cis/trans isomerases that can control receptor-mediated intracellular signaling. The prototypic PPIase FKBP12 functionally interacts with EGFR. FKBP12 was shown to inhibit EGF-induced EGFR autophosphorylation with all internal phosphorylation sites equally affected. The inhibition of EGFR catalytic activity is conducted by targeting the EGFR kinase domain. The change of intracellular FKBP12 levels resulted in a change of EGFR autophosphorylation level. Collectively, our results demonstrate that FKBP12 forms an endogenous inhibitor of EGFR phosphorylation directly involved in the control of cellular EGFR activity.
ACS Publications