Abstract:
<jats:p>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<jats:sup>32</jats:sup>P release and a point mutant of Thr 38.</jats:p>
Description:
<jats:p>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<jats:sup>32</jats:sup>P release and a point mutant of Thr 38.</jats:p>