Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase
Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase
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DOI：
10.1016/s0014-5793(01)02277-3
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发表时间：
2001-03-30
期刊：
影响因子：
3.5
通讯作者：
Haystead, TAJ
中科院分区：
文献类型：
--
作者：
MacDonald, JA;Eto, M;Haystead, TAJ
研究了通过MYPT 1相关激酶（M110激酶）对CPI-17和PHI-1的磷酸化。M110激酶是最近发现的一种丝氨酸/苏氨酸激酶，其催化结构域与ZIP激酶的催化结构域同源（ZIPK，GST-rN-ZIPk，一种组成型活性GST融合片段，将CPI-17（但不包括PHI-1）磷酸化至化学计量为1.7 mol/mol，磷酸化氨基酸分析显示Ser和Thr残基的磷酸化，CPI-17中的磷酸化位点使用Edman测序与P-32释放和Thr 38的点突变体鉴定为Thr 38和Ser 12，（C）2001由Elsevier Science B. V.代表欧洲生物化学学会联合会出版。
Phosphorylation of CPI-17 and PHI-1 by the MYPT1-associated kinase (M110 kinase) was investigated. M110 kinase is a recently identified serine/threonine kinase with a catalytic domain that is homologous to that of ZIP kinase (ZIPK, GST-rN-ZIPk, a constitutively active GST fusion fragment, phosphorylates CPI-17 (but not PHI-1) to a stoichiometry of 1.7 mol/mol, Phosphoamino acid analysis revealed phosphorylation of both Ser and Thr residues, Phosphorylation sites in CPI-17 were identified as Thr 38 and Ser 12 using Edman sequencing with P-32 release and a point mutant of Thr 38, (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.