Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin

Attila Tóth, Enikö Kiss, P. Gergely, Michael P. Walsh, David J. Hartshorne, F. Erdődi

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The effect of phosphorylation in the N-terminal region of myosin phosphatase target subunit 1 (MYPT1) on the interactions with protein phosphatase 1 catalytic subunit (PP1c) and with phosphorylated 20 kDa myosin light chain (P-MLC20) was studied. Protein kinase C (PKC) phosphorylated threonine-34 (1 mol/mol), the residue preceding the consensus PP1c-binding motif (35KVKF38) in MYPT11-38, but this did not affect binding of the peptide to PP1c. PKC incorporated 2 mol P(i) into MYPT11-296 suggesting a second site of phosphorylation within the ankyrin repeats (residues 40-296). This phosphorylation diminished the stimulatory effect of MYPT11-296 on the P-MLC20 phosphatase activity of PP1c. Binding of PP1c or P-MLC20 to phosphorylated MYPT11-296 was also attenuated. It is concluded that phosphorylation of MYPT1 by PKC may therefore result in altered dephosphorylation of myosin. Copyright (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)113-117
Number of pages5
JournalFEBS Letters
Volume484
Issue number2
DOIs
Publication statusPublished - Nov 3 2000

Fingerprint

Myosin-Light-Chain Phosphatase
Protein Phosphatase 1
Myosin Light Chains
Phosphorylation
Protein Kinase C
Catalytic Domain
Ankyrin Repeat
Threonine
Myosins
Phosphoric Monoester Hydrolases
Carrier Proteins
Peptides

Keywords

  • Ankyrin repeat
  • Myosin phosphatase
  • Myosin phosphatase target subunit 1
  • Protein kinase C
  • Protein phosphatase 1

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin. / Tóth, Attila; Kiss, Enikö; Gergely, P.; Walsh, Michael P.; Hartshorne, David J.; Erdődi, F.

In: FEBS Letters, Vol. 484, No. 2, 03.11.2000, p. 113-117.

Research output: Contribution to journalArticle

Tóth, Attila ; Kiss, Enikö ; Gergely, P. ; Walsh, Michael P. ; Hartshorne, David J. ; Erdődi, F. / Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin. In: FEBS Letters. 2000 ; Vol. 484, No. 2. pp. 113-117.
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AU - Hartshorne, David J.

AU - Erdődi, F.

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AB - The effect of phosphorylation in the N-terminal region of myosin phosphatase target subunit 1 (MYPT1) on the interactions with protein phosphatase 1 catalytic subunit (PP1c) and with phosphorylated 20 kDa myosin light chain (P-MLC20) was studied. Protein kinase C (PKC) phosphorylated threonine-34 (1 mol/mol), the residue preceding the consensus PP1c-binding motif (35KVKF38) in MYPT11-38, but this did not affect binding of the peptide to PP1c. PKC incorporated 2 mol P(i) into MYPT11-296 suggesting a second site of phosphorylation within the ankyrin repeats (residues 40-296). This phosphorylation diminished the stimulatory effect of MYPT11-296 on the P-MLC20 phosphatase activity of PP1c. Binding of PP1c or P-MLC20 to phosphorylated MYPT11-296 was also attenuated. It is concluded that phosphorylation of MYPT1 by PKC may therefore result in altered dephosphorylation of myosin. Copyright (C) 2000 Federation of European Biochemical Societies.

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