pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity

pp54 microtubule-associated protein-2 (MAP-2) kinase, a recently discovered protein serine/threonine kinase (Kyriakis, J., and Avruch, J. (1990) J. Biol. Chem. 265, 17355-17363), is shown to contain immunoreactive phosphotyrosine residues. Treatment with recombinant rat brain protein tyrosine phosph...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 266; no. 16; pp. 10043 - 10046
Main Authors:	KYRIAKIS, J. M, BRAUTIGAN, D. L, INGEBRITSEN, T. S, AVRUCH, J
Format:	Journal Article
Language:	English
Published:	Bethesda, MD American Society for Biochemistry and Molecular Biology 05-06-1991
Subjects:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Blotting, Western Brain - enzymology Calcium-Calmodulin-Dependent Protein Kinases CDC2 Protein Kinase - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Phosphoprotein Phosphatases - pharmacology Phosphorylation Precipitin Tests Protein Kinase Inhibitors Protein Kinases - metabolism Protein Phosphatase 1 Rabbits Rats serine Serine - metabolism Threonine - metabolism Transferases tyrosine Tyrosine - metabolism Immunoprecipitation reaction Phosphorylation Regulation(control) Enzymatic activity Enzyme Protein kinase Aminoacid Microtubule associated protein
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Summary:	pp54 microtubule-associated protein-2 (MAP-2) kinase, a recently discovered protein serine/threonine kinase (Kyriakis, J., and Avruch, J. (1990) J. Biol. Chem. 265, 17355-17363), is shown to contain immunoreactive phosphotyrosine residues. Treatment with recombinant rat brain protein tyrosine phosphatase-1 deactivates pp54 MAP-2 kinase, concomitant with the removal of phosphotyrosine residues. Protein (serine/threonine) phosphatase-1 also deactivates pp54 MAP-2 kinase in a specific fashion. pp54 MAP-2 kinase joins pp42 MAP-2 kinase and cdc2/maturation-promoting factor as one of only three serine/threonine protein kinases known to be regulated by phosphorylation at both tyrosine and, independently, at serine/threonine residues. In view of these shared regulatory properties, a role for pp54 MAP-2 kinase in the control of cell division is likely.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0021-9258 1083-351X
DOI:	10.1016/S0021-9258(18)99183-0