Evidence map›Paper›PMID 18155661›Full record

ReviewBiochemical and biophysical research communications2008

Myosin phosphatase target subunit: Many roles in cell function.

Fumio Matsumura, David J Hartshorne

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical and biophysical research communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

122 citing papers in PubMed, 182 citations in OpenAlex.

  1. Review
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  16. Mfge8 attenuates human gastric antrum smooth muscle contractions.Journal of muscle research and cell motility · 2021
    Article
  17. Article
  18. Article
  19. TheMolecular biology of the cell · 2020
    Article
  20. Article

62 more citing papers are in PubMed but not listed here.

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 1 country.

Fumio MatsumuraDepartment of Molecular Biology and Biochemistry, Rutgers University, 604, Allison Road, Piscataway, NJ 08855, USA.
David J Hartshorne
Rutgers, The State University of New Jersey · USUniversity of Arizona · US

Funding

TROPOMYOSINS IN NORMAL AND TRANSFORMED CELLSR01CA042742 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MATSUMURA, FUMIO · 1985 to 2009
$3.6M
BIOCHEMISTRY OF CONTRACTILE PROTEINSR01HL023615 · NHLBI · UNIVERSITY OF ARIZONA · PI HARTSHORNE, DAVID JOHN · 1985 to 2009
$2.8M
MICROFILAMENT ORGANIZATION DURING MITOSIS AND CELL TRANSR37CA042742 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MATSUMURA, FUMIO · 1991 to 1999
–
NCI NIH HHS CA 42742NCI NIH HHS R01 CA042742NCI NIH HHS R37 CA042742NHLBI NIH HHS HL 23615NHLBI NIH HHS R01 HL023615
6 · The paper itself

Abstract

Phosphorylation of myosin II is important in many aspects of cell function and involves a myosin kinase, e.g. myosin light chain kinase, and a myosin phosphatase (MP). MP is regulated by the myosin phosphatase target subunit (MYPT1). The domain structure, properties, and genetic analyses of MYPT1 and its isoforms are outlined. MYPT1 binds the catalytic subunit of type 1 phosphatase, delta isoform, and also acts as an interactive platform for many other proteins. A key reaction for MP is with phosphorylated myosin II and the first process shown to be regulated by MP was contractile activity of smooth muscle. In cell division and cell migration myosin II phosphorylation also plays a critical role and these are discussed. However, based on the wide range of partners for MYPT1 it is likely that MP is implicated with substrates other than myosin II. Open questions are whether the diverse functions of MP reflect different cellular locations and/or specific roles for the MYPT1 isoforms.

Indexed as

Models, BiologicalCell DivisionCell MovementEnzyme ActivationMyosin-Light-Chain PhosphataseMyosin Type IIPhosphorylationMyosin-Light-Chain PhosphataseMyosin Type IIPPP1R12A protein, human

Identifiers

PMID18155661
PMCPMC2367208
OpenAlexW1984994493

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.