Premium
Identification of serines‐1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites
Author(s) -
Liu Feng,
Roth Richard A.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00996-1
Subject(s) - cyclin dependent kinase 9 , phosphorylation , insulin receptor , chemistry , mitogen activated protein kinase kinase , protein kinase domain , map kinase kinase kinase , kinase , protein kinase a , microbiology and biotechnology , biochemistry , insulin , biology , endocrinology , insulin resistance , gene , mutant
A new site of serine phosphorylation (Ser‐1035/1037) has been identified in the kinase domain of the insulin receptor. Mutant receptors missing these two serines were expressed in Chinese hamster ovary cells overexpressing protein kinase Cα. These mutant receptors lacked a phorbol ester‐stimulated phosphoserine containing tryptic peptide as demonstrated by both high percentage polyacrylamide/urea gel electrophoresis and two‐dimensional tlc. Moreover, a synthetic peptide with the sequence of this tryptic peptide was phosphorylated by isolated protein kinase Cα, and co‐migrated with the phosphopeptide from in vivo labeled receptor. These results indicate that serine‐1035 and/or 1037 in the kinase domain of the insulin receptor are phosphorylated in response to activation of protein kinase Cα.