Dual Ser and Thr phosphorylation of CPI‐17, an inhibitor of myosin phosphatase, by MYPT‐associated kinase

FEBS Letters

Eto, Masumi²  Haystead, Timothy A.J.³  Borman, Meredith A.¹  Brautigan, David L.²  MacDonald, Justin A.³ 

[1] Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908, USA;Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908, USA;Department of Pharmacology and Cancer Biology, Duke University Medical Center, P.O. Box 3813, Durham, NC 27710, USA

关键词: CPI-17;    M110 kinase;    Myosin phosphatase;    Calcium sensitization;    Smooth muscle;   

DOI  :  10.1016/S0014-5793(01)02277-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ³²P release and a point mutant of Thr 38.

【 授权许可】

Unknown