Evidence map›Paper›PMID 10037794›Full record

ArticleThe Journal of cell biology1999

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation.

G Totsukawa, Y Yamakita, S Yamashiro, H Hosoya, D J Hartshorne, F Matsumura

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 63 citations in OpenAlex.

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  16. Myosin phosphatase target subunit: Many roles in cell function.Biochemical and biophysical research communications · 2008
    Review
  17. Caldesmon and the regulation of cytoskeletal functions.Advances in experimental medicine and biology · 2008
    Review
  18. Localization of myosin phosphatase target subunit and its mutants.Journal of muscle research and cell motility · 2005
    Article
  19. 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

6 authors at 2 institutions in 2 countries.

G TotsukawaDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08855, USA.
Y Yamakita
S Yamashiro
H Hosoya
D J Hartshorne
F Matsumura
University of Arizona · USRutgers, The State University of New Jersey · 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 CA42742NCI NIH HHS R01 CA042742NCI NIH HHS R37 CA042742NHLBI NIH HHS HL23615NHLBI NIH HHS R01 HL023615
6 · The paper itself

Abstract

It has been demonstrated previously that during mitosis the sites of myosin phosphorylation are switched between the inhibitory sites, Ser 1/2, and the activation sites, Ser 19/Thr 18 (Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. J. Cell Biol. 124:129- 137; Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. J. Cell Biol. 118:595-605), suggesting a regulatory role of myosin phosphorylation in cell division. To explore the function of myosin phosphatase in cell division, the possibility that myosin phosphatase activity may be altered during cell division was examined. We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mitosis-specific phosphorylation and that the phosphorylation is reversed during cytokinesis. MYPT phosphorylated either in vivo or in vitro in the mitosis-specific way showed higher binding to myosin II (two- to threefold) compared to MYPT from cells in interphase. Furthermore, the activity of myosin phosphatase was increased more than twice and it is suggested this reflected the increased affinity of myosin binding. These results indicate the presence of a unique positive regulatory mechanism for myosin phosphatase in cell division. The activation of myosin phosphatase during mitosis would enhance dephosphorylation of the myosin regulatory light chain, thereby leading to the disassembly of stress fibers during prophase. The mitosis-specific effect of phosphorylation is lost on exit from mitosis, and the resultant increase in myosin phosphorylation may act as a signal to activate cytokinesis.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesCell LineChickensCHO CellsCricetinaeDNA PrimersInterphaseIn Vitro TechniquesMitosisMolecular Sequence DataMyosin-Light-Chain PhosphataseMyosinsPhosphoprotein PhosphatasesDNA PrimersMyosin-Light-Chain PhosphataseMyosinsPhosphoprotein Phosphatases

Identifiers

PMID10037794
PMCPMC2132942
OpenAlexW2000562368

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
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.