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J. Biol. Chem., Vol. 266, Issue 16, 10043-10046, 06, 1991
JM Kyriakis, DL Brautigan, TS Ingebritsen and J Avruch
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.
pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity
Diabetes Unit and Medical Services, Massachusetts General Hospital, Boston.
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