October 31, 2000FEBS LettersOpen Access

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

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Population

In vitro biochemical model studying myosin phosphatase target subunit 1, protein phosphatase 1 catalytic…

Design

Preclinical

Authors

ATAttila TóthUniversity of Debrecen EKEnikö KissUniversity of Szeged PGPál GergelyUniversity of Debrecen

Discussion

Member takes

Implication

Hypothesis-generating for PKC-MYPT1 regulation of myosin dephosphorylation; requires human validation before clinical consideration.

Structured PICO

Population

In vitro biochemical model studying myosin phosphatase target subunit 1 (MYPT1), protein phosphatase 1 catalytic subunit (PP1c), and phosphorylated 20 kDa myosin light chain (P-MLC20)

Intervention

Phosphorylation of MYPT1 by protein kinase C (PKC)

Outcome

Effect of phosphorylation on interactions with PP1c and P-MLC20, and phosphatase activitysurrogate

Phosphorylation of MYPT1 by PKC attenuates its interaction with PP1c and P-MLC20, suggesting a mechanism for altered dephosphorylation of myosin.

Cite This Study

Tóth et al. (2000) studied this question.

synapsesocial.com/papers/6a8d2891dafbba8333314ebf https://doi.org/10.1016/s0014-5793(00)02138-4

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

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider