Evidence map›Paper›PMID 8294496›Full record

ArticleThe Journal of cell biology1994

In vivo phosphorylation of regulatory light chain of myosin II during mitosis of cultured cells.

Y Yamakita, S Yamashiro, F Matsumura

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 152 citations in OpenAlex.

  1. Article
  2. Article
  3. Myosin light chain kinase is a potential target for hypopharyngeal cancer treatment.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2020
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. A transcribed pseudogene of MYLK promotes cell proliferation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  15. Article
  16. Understanding cytokinesis failure.Advances in experimental medicine and biology · 2010
    Review
  17. Article
  18. Article
  19. Article
  20. Article

6 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

3 authors at 1 institution in 1 country.

Y YamakitaDepartment of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08855-1059.
S Yamashiro
F Matsumura
Rutgers, The State University of New Jersey · US

Funding

TROPOMYOSINS IN NORMAL AND TRANSFORMED CELLSK04CA001304 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MATSUMURA, FUMIO · 1988 to 1992
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MICROFILAMENT ORGANIZATION DURING MITOSIS AND CELL TRANSR37CA042742 · NCI · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MATSUMURA, FUMIO · 1991 to 1999
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NCI NIH HHS K04 CA01304NCI NIH HHS R37 CA42742
6 · The paper itself

Abstract

Phosphorylation of the regulatory light chain of myosin II (MLC) controls the contractility of actomyosin in nonmuscle and muscle cells. It has been reported that cdc2 phosphorylates MLC in vitro at Ser-1 or Ser-2 and Thr-9 which protein kinase C phosphorylates (Satterwhite, L. L., M. J. Lohka, K. L. Wilson, T. Y. Scherson, L. K. Cisek, J. L. Corden, and T. D. Pollard. 1992 J. Cell Biol. 118:595-605). We have examined in vivo phosphorylation of MLC during mitosis and after the release of mitotic arrest. Phosphate incorporation of MLC in mitotic cells is found to be 6-12 times greater than that in nonmitotic cells. Phosphopeptide maps have revealed that the MLC from mitotic cells is phosphorylated at Ser-1 and/or Ser-2 (Ser-1/2), but not at Thr-9. MLC is also phosphorylated to a much lesser extent at Ser-19 which myosin light chain kinase phosphorylates. On the other hand, MLC of nonmitotic cells is phosphorylated at Ser-19 but not at Ser-1/2. The extent of phosphate incorporation is doubled at 30 min after the release of mitotic arrest when some cells start cytokinesis. Phosphopeptide analyses have revealed that the phosphorylation at Ser-19 is increased 20 times, while the phosphorylation at Ser-1/2 is decreased by half. This high extent of MLC phosphorylation at Ser-19 is maintained for another 30 min and gradually decreased to near the level of interphase cells as cells complete spreading at 180 min. On the other hand, phosphorylation at Ser-1/2 is decreased to 18% at 60 min, and is practically undetectable at 180 min after the release of mitotic arrest. The stoichiometry of MLC phosphorylation has been determined by quantitation of phosphorylated and unphosphorylated forms of MLC separated on 2D gels. The molar ratio of phosphorylated MLC to total MLC is found to be 0.16 +/- 0.06 and 0.31 +/- 0.05 in interphase and mitotic cells, respectively. The ratio is increased to 0.49 +/- 0.05 at 30 min after the release of mitotic arrest. These results suggest that the change in the phosphorylation site from Ser-1/2 to Ser-19 plays an important role in signaling cytokinesis.

Indexed as

MitosisAnimalsCDC2 Protein KinaseCell CompartmentationCell DivisionCells, CulturedChickensElectrophoresis, Gel, Two-DimensionalHeLa CellsHumansIn Vitro TechniquesMyosin-Light-Chain KinaseMyosinsPeptide MappingPhosphoproteinsPhosphorylationCDC2 Protein KinaseMyosin-Light-Chain KinaseMyosinsPhosphoproteins

Identifiers

PMID8294496
PMCPMC2119899
OpenAlexW1982301053

What OpenQuestion holds

Textmetadata
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.