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

作者：John M. Kyriakis, David L. Brautigan, Thomas S. Ingebritsen, Joseph Avruch · 发表于：Journal of Biological Chemistry · 年份：1991 · DOI：10.1016/s0021-9258(18)99183-0 · 被引用次数：108 · 研究领域：Protein Tyrosine Phosphatases、Microtubule and mitosis dynamics、Protein Kinase Regulation and GTPase Signaling

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.