• Media type: E-Article
  • Title: Dual Ser and Thr phosphorylation of CPI‐17, an inhibitor of myosin phosphatase, by MYPT‐associated kinase
  • Contributor: MacDonald, Justin A.; Eto, Masumi; Borman, Meredith A.; Brautigan, David L.; Haystead, Timothy A.J.
  • Published: Wiley, 2001
  • Published in: FEBS Letters
  • Extent: 91-94
  • Language: English
  • DOI: 10.1016/s0014-5793(01)02277-3
  • ISSN: 0014-5793; 1873-3468
  • Keywords: Cell Biology ; Genetics ; Molecular Biology ; Biochemistry ; Structural Biology ; Biophysics
  • 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>
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  • Access State: Open Access