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

2001/03/30 by Justin A. MacDonald, Masumi Eto, Meredith A. Borman +3 · 18 citations
Biochemistry, Genetics and Molecular Biology · #Protein Kinase Regulation and GTPase Signaling #Cellular transport and secretion #Ion channel regulation and function

paper · pdf · doi:10.1016/s0014-5793(01)02277-3

Abstract

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 (32)P release and a point mutant of Thr 38.

Citations

• Phosphorylation of CPI‐17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho‐kinase

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