Phosphorylation of microtubule-associated protein 2 by MAP kinase primarily involves the projection domain.
Chymotryptic digestion was used to localize the sites in microtubule-associated protein 2 which are preferentially phosphorylated in vitro by MAP kinase, an insulin-stimulated serine/threonine kinase which efficiently utilizes high molecular weight MAPs as substrates. MAP kinase phosphorylates sites in the projection domain almost exclusively; less than 6% of the phosphate incorporated by MAP kinase was found in the tubulin binding domain. This site specificity is in marked contrast to that of the catalytic subunit of cAMP dependent protein kinase, and most other protein kinases phosphorylating MAP-2, which extensively phosphorylate the tubulin binding domain.
Silliman
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CC
Department of Pediatrics, University of Virginia School of Medicine, Charlottesville 22908.
Sturgill
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TW
D000818:Animals; D001665:Binding Sites; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology; D007700:Kinetics; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010446:Peptide Fragments; D010710:Phosphates / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D014404:Tubulin / Q000378:metabolism
D008869:Microtubule-Associated Proteins; D010446:Peptide Fragments; D010710:Phosphates; D014404:Tubulin; D000242:Cyclic AMP; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002918:Chymotrypsin