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The paradoxical regulation of protein phosphorylation in insulin action
Author(s) -
Saltiel Alan R.
Publication year - 1994
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.8.13.7926368
Subject(s) - phosphorylation , protein phosphorylation , insulin , tyrosine phosphorylation , insulin receptor , dephosphorylation , microbiology and biotechnology , phosphorylation cascade , signal transduction , biology , protein kinase a , chemistry , biochemistry , endocrinology , insulin resistance , phosphatase
Many cellular actions of insulin are mediated by changes in protein phosphorylation. The consequences of these phosphorylation events extend from a series of different short‐term metabolic actions to longer‐term effects of the hormone on cellular growth and differentiation. Although the insulin receptor itself is a tyrosine kinase that is activated upon hormone binding, the ensuing changes in phosphorylation occur predominantly on serine and threonine residues. Moreover, insulin can simultaneously stimulate the phosphorylation of some proteins and the dephosphorylation of others. These paradoxical effects of insulin suggest that separate signal transduction pathways may emanate from the receptor itself to produce the pleiotropic actions of the hormone.—Saltiel, A. R. The paradoxical regulation of protein phosphorylation in insulin action. FASEB J. 8: 1034‐1040; 1994.