Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin
Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin
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 Pi 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.
- University of Calgary Canada
- University of Arizona United States
- University and National Library University of Debrecen Hungary
- Univesity of Debrecen Hungary
- University of Debrecen Hungary
Myosin Light Chains, Myosin phosphatase target subunit 1, Orvostudományok, Ankyrin repeat, Myosin phosphatase, Ankyrin Repeat, Molecular Weight, Myosin-Light-Chain Phosphatase, Protein phosphatase 1, Protein kinase C, Catalytic Domain, Protein Phosphatase 1, Phosphoprotein Phosphatases, Animals, Elméleti orvostudományok, Rabbits, Phosphorylation, Peptides, Protein Kinase C
Myosin Light Chains, Myosin phosphatase target subunit 1, Orvostudományok, Ankyrin repeat, Myosin phosphatase, Ankyrin Repeat, Molecular Weight, Myosin-Light-Chain Phosphatase, Protein phosphatase 1, Protein kinase C, Catalytic Domain, Protein Phosphatase 1, Phosphoprotein Phosphatases, Animals, Elméleti orvostudományok, Rabbits, Phosphorylation, Peptides, Protein Kinase C
4 Research products, page 1 of 1
- 2017IsAmongTopNSimilarDocuments
- 2023IsAmongTopNSimilarDocuments
- 2010IsAmongTopNSimilarDocuments
- 2017IsRelatedTo
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).40 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
