pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity.
pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity.
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DOI：
10.1016/s0021-9258(18)99183-0
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发表时间：
1991-06
期刊：
影响因子：
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通讯作者：
J. Kyriakis;D. Brautigan;T. Ingebritsen;J. Avruch
中科院分区：
文献类型：
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作者：
J. Kyriakis;D. Brautigan;T. Ingebritsen;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.
