Evidence map›Paper›PMID 20130087›Full record

ArticleMolecular biology of the cell2010

Par-4: a new activator of myosin phosphatase.

Susanne Vetterkind, Eunhee Lee, Eric Sundberg, Ransom H Poythress, Terence C Tao, Ute Preuss, Kathleen G Morgan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Regulation of myosin light-chain phosphorylation and its roles in cardiovascular physiology and pathophysiology.Hypertension research : official journal of the Japanese Society of Hypertension · 2022
    Review
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  5. Review
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  8. MYPT1 isoforms expressed in HEK293T cells are differentially phosphorylated after GTPγS treatment.Journal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016
    Article
  9. Article
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  11. Hierarchical scaffolding of an ERK1/2 activation pathway.Cell communication and signaling : CCS · 2013
    Article
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  13. Article
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  15. Article
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  18. AnBioTechniques
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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

7 authors at 3 institutions in 2 countries.

Susanne VetterkindDepartment of Health Sciences, Sargent College of Health and Rehabilitation Sciences, Boston University, Boston, MA 02215, USA.
Eunhee Lee
Eric Sundberg
Ransom H Poythress
Terence C Tao
Ute Preuss
Kathleen G Morgan
Boston Biomedical Research Institute · USBoston University · USUniversity of Bonn · DE

Funding

Structure-Function of the CytoskeletonP01HL086655 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2007 to 2011
$8.8M
REGULATION OF CONTRACTION OF BLOOD VESSELSR01HL031704 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 1985 to 2009
$3.7M
Mechanism of Calcium Regulation in Striated MuscleR01AR049066 · NIAMS · BOSTON BIOMEDICAL RESEARCH INSTITUTE · PI TAO, TERENCE · 2003 to 2007
$3.2M
Subcellular Organization of Signaling in Smooth MuscleR01HL080003 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI MORGAN, KATHLEEN G · 2006 to 2009
$1.7M
NHLBI NIH HHS HL-31704NHLBI NIH HHS HL-80003NHLBI NIH HHS HL-86655NHLBI NIH HHS P01 HL086655NHLBI NIH HHS R01 HL031704NHLBI NIH HHS R01 HL080003NIAMS NIH HHS AR-49066NIAMS NIH HHS R01 AR049066
6 · The paper itself

Abstract

Myosin phosphatase (MP) is a key regulator of myosin light chain (LC20) phosphorylation, a process essential for motility, apoptosis, and smooth muscle contractility. Although MP inhibition is well studied, little is known about MP activation. We have recently demonstrated that prostate apoptosis response (Par)-4 modulates vascular smooth muscle contractility. Here, we test the hypothesis that Par-4 regulates MP activity directly. We show, by proximity ligation assays, surface plasmon resonance and coimmunoprecipitation, that Par-4 interacts with the targeting subunit of MP, MYPT1. Binding is mediated by the leucine zippers of MYPT1 and Par-4 and reduced by Par-4 phosphorylation. Overexpression of Par-4 leads to increased phosphatase activity of immunoprecipitated MP, whereas small interfering RNA knockdown of endogenous Par-4 significantly decreases MP activity and increases MYPT1 phosphorylation. LC20 phosphorylation assays demonstrate that overexpression of Par-4 reduces LC20 phosphorylation. In contrast, a phosphorylation site mutant, but not wild-type Par-4, interferes with zipper-interacting protein kinase (ZIPK)-mediated MP inhibition. We conclude from our results Par-4 operates through a "padlock" model in which binding of Par-4 to MYPT1 activates MP by blocking access to the inhibitory phosphorylation sites, and inhibitory phosphorylation of MYPT1 by ZIPK requires "unlocking" of Par-4 by phosphorylation and displacement of Par-4 from the MP complex.

Indexed as

AnimalsAortaApoptosisApoptosis Regulatory ProteinsCell ProliferationDNAElectrophoresis, Gel, Two-DimensionalEnzyme ActivationMicroscopy, FluorescenceMuscle, Smooth, VascularMyosin-Light-Chain PhosphatasePhosphorylationRatsRNAApoptosis Regulatory ProteinsDNAMyosin-Light-Chain Phosphataseprostate apoptosis response-4 proteinRNA

Identifiers

PMID20130087
PMCPMC2847525
OpenAlexW2133335227

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.