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Evidence that the insulin receptor‐associated protein kinase acts as a phosphatidylinositol kinase
Author(s) -
Machicao E.,
Wieland O.H.
Publication year - 1984
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(84)80581-5
Subject(s) - insulin receptor , phosphatidylinositol , insulin receptor substrate , irs2 , receptor tyrosine kinase , tyrosine kinase , tropomyosin receptor kinase c , chemistry , insulin , microbiology and biotechnology , signal transduction , biochemistry , biology , receptor , endocrinology , platelet derived growth factor receptor , insulin resistance , growth factor
Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin‐stimulated phosphate incorporation from [γ‐ 32 P]ATP into endogenous (membrane) and exogenous phosphatidylinositol. Our data suggest that the insulin receptor associated protein (tyrosine) kinase can act as a phosphatidylinsositol kinase, and that this mechanism may be of physiological importance in signal transduction of insulin.