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Title: Insulin-stimulated microtubule-associated protein kinase is phosphorylated on tyrosine and threonine in vivo

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
;  [1]
  1. Univ. of Virginia School of Medicine, Charlottesville (USA)

Exposure of 3T3-L1 cells to insulin stimulates a soluble, serine(threonine)-specific protein kinase that phosphorylates microtubule-associated protein 2 (MAP-2) in vitro. The enzyme, termed MAP kinase, was isolated from insulin-treated or control cells radiolabeled with {sup 32}P{sub i}. A 40-kDa phosphoprotein was found to elute in exact correspondence with enzymatic activity during hydrophobic interaction and gel filtration chromatography of extracts from cells stimulated with insulin. Both MAP kinase activity and the phosphoprotein were absent in fractions prepared from untreated cells. The {sup 32}P incorporated into the 40-kDa protein was stable during treatment with alkali. Phospho amino acid analysis confirmed that the radiolabel was primarily incorporated into phosphotyrosine and to a lesser extend phosphothreonine. In addition, MAP kinase was incompletely but specifically adsorbed by antibodies to phosphotyrosine. The authors conclude, based on these data and additional studies from this laboratory, that MAP kinase is phosphorylated on tyrosine in vivo. The data are consistent with the possibility that MAP kinase may be a substrate for the insulin receptor or another insulin-regulated tyrosine kinase.

OSTI ID:
5365254
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 85:11; ISSN 0027-8424
Country of Publication:
United States
Language:
English

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