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The APS adapter protein couples the insulin receptor to the phosphorylation of c‐Cbl and facilitates ligand‐stimulated ubiquitination of the insulin receptor
Author(s) -
Ahmed Z,
Smith B.J,
Pillay T.S
Publication year - 2000
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/s0014-5793(00)01621-5
Subject(s) - insulin receptor , insulin receptor substrate , irs2 , grb10 , insulin , phosphorylation , receptor , insulin like growth factor 1 receptor , ubiquitin , tyrosine phosphorylation , chemistry , biology , microbiology and biotechnology , endocrinology , biochemistry , insulin resistance , growth factor , gene
The APS adapter protein is rapidly tyrosine‐phosphorylated following insulin stimulation. In insulin‐stimulated 3T3‐L1 adipocytes, APS co‐precipitated with phosphorylated c‐Cbl. In CHO.T‐APS cells overexpressing the insulin receptor and APS, APS co‐precipitated with c‐Cbl but not in CHO.T cells which do not express APS. APS‐mediated recruitment of c‐Cbl to the insulin receptor led to rapid ubiquitination of the insulin receptor β‐subunit in CHO.T‐APS but not in parental CHO.T cells. These results suggest that the function of APS is to facilitate coupling of the insulin receptor to c‐Cbl in order to catalyse the ubiquitination of the receptor and initiation of internalisation or degradation.