Evidence map›Paper›PMID 18094049›Full record

ArticleMolecular biology of the cell2008

A novel regulatory mechanism of myosin light chain phosphorylation via binding of 14-3-3 to myosin phosphatase.

Yasuhiko Koga, Mitsuo Ikebe

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Arsenic disrupts extracellular vesicle-mediated signaling in regenerating myofibers.Toxicological sciences : an official journal of the Society of Toxicology · 2023
    Article
  4. Article
  5. 14-3-3 protein regulation of excitation-contraction coupling.Pflugers Archiv : European journal of physiology · 2022
    Review
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  19. 14-3-3 proteins regulate protein kinase a activity to modulate growth cone turning responses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Yasuhiko KogaDepartment of Physiology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Mitsuo Ikebe
Gunma University · JPUniversity of Massachusetts Chan Medical School · US

Funding

Regulation of Myosin Phosphorylation in Smooth MuscleR01HL073050 · NHLBI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2013
$4.0M
Regulation of Mammalian Class VI MyosinR01AR048526 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Function of Small G-Protein Binding MyosinR01AR048898 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.8M
Motor Function and Regulation of Myosin VIIR01DC006103 · NIDCD · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI IKEBE, MITSUO · 2003 to 2007
$1.5M
NHLBI NIH HHS HL 073050NHLBI NIH HHS R01 HL073050NIAMS NIH HHS AR 048526NIAMS NIH HHS AR 048898NIAMS NIH HHS R01 AR048526NIAMS NIH HHS R01 AR048898NIDCD NIH HHS DC 006103NIDCD NIH HHS R01 DC006103
6 · The paper itself

Abstract

Myosin II phosphorylation-dependent cell motile events are regulated by myosin light-chain (MLC) kinase and MLC phosphatase (MLCP). Recent studies have revealed myosin phosphatase targeting subunit (MYPT1), a myosin-binding subunit of MLCP, plays a critical role in MLCP regulation. Here we report the new regulatory mechanism of MLCP via the interaction between 14-3-3 and MYPT1. The binding of 14-3-3beta to MYPT1 diminished the direct binding between MYPT1 and myosin II, and 14-3-3beta overexpression abolished MYPT1 localization at stress fiber. Furthermore, 14-3-3beta inhibited MLCP holoenzyme activity via the interaction with MYPT1. Consistently, 14-3-3beta overexpression increased myosin II phosphorylation in cells. We found that MYPT1 phosphorylation at Ser472 was critical for the binding to 14-3-3. Epidermal growth factor (EGF) stimulation increased both Ser472 phosphorylation and the binding of MYPT1-14-3-3. Rho-kinase inhibitor inhibited the EGF-induced Ser472 phosphorylation and the binding of MYPT1-14-3-3. Rho-kinase specific siRNA also decreased EGF-induced Ser472 phosphorylation correlated with the decrease in MLC phosphorylation. The present study revealed a new RhoA/Rho-kinase-dependent regulatory mechanism of myosin II phosphorylation by 14-3-3 that dissociates MLCP from myosin II and attenuates MLCP activity.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsHumansMiceModels, BiologicalMolecular Sequence DataMyosin-Light-Chain PhosphataseMyosin Light ChainsMyosin Type IINIH 3T3 CellsPhosphorylationPhosphoserineProtein Binding14-3-3 ProteinsMyosin-Light-Chain PhosphataseMyosin Light ChainsMyosin Type IIPhosphoserinePpp1r12a protein, ratProtein Phosphatase 1YWHAB protein, human

Identifiers

PMID18094049
PMCPMC2262977
OpenAlexW2159856430

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.