Evidence map›Paper›PMID 11062269›Full record

ArticleThe Journal of cell biology2000

Localization and activity of myosin light chain kinase isoforms during the cell cycle.

A Poperechnaya, O Varlamova, P J Lin, J T Stull, A R Bresnick

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

41 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. WNK1 Kinase Activity Is Required for the Functional Maintenance of Podocyte Structure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. CaCurrent biology : CB · 2025
    Article
  4. Postnatal development alters functional compartmentalization of myosin light chain kinase in ovine carotid arteries.American journal of physiology. Regulatory, integrative and comparative physiology · 2021
    Article
  5. Review
  6. Article
  7. Energy-Mediated Machinery Drives Cellular Mechanical Allostasis.Advanced materials (Deerfield Beach, Fla.) · 2019
    Article
  8. Article
  9. WDR5 modulates cell motility and morphology and controls nuclear changes induced by a 3D environment.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Nonmuscle myosin-2: mix and match.Cellular and molecular life sciences : CMLS · 2013
    Review
  16. Article
  17. Article
  18. 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

5 authors at 2 institutions in 1 country.

A PoperechnayaDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
O Varlamova
P J Lin
J T Stull
A R Bresnick
Albert Einstein College of Medicine · USThe University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation on Ser 19 of the myosin II regulatory light chain by myosin light chain kinase (MLCK) regulates actomyosin contractility in smooth muscle and vertebrate nonmuscle cells. The smooth/nonmuscle MLCK gene locus produces two kinases, a high molecular weight isoform (long MLCK) and a low molecular weight isoform (short MLCK), that are differentially expressed in smooth and nonmuscle tissues. To study the relative localization of the MLCK isoforms in cultured nonmuscle cells and to determine the spatial and temporal dynamics of MLCK localization during mitosis, we constructed green fluorescent protein fusions of the long and short MLCKs. In interphase cells, localization of the long MLCK to stress fibers is mediated by five DXRXXL motifs, which span the junction of the NH(2)-terminal extension and the short MLCK. In contrast, localization of the long MLCK to the cleavage furrow in dividing cells requires the five DXRXXL motifs as well as additional amino acid sequences present in the NH(2)-terminal extension. Thus, it appears that nonmuscle cells utilize different mechanisms for targeting the long MLCK to actomyosin structures during interphase and mitosis. Further studies have shown that the long MLCK has twofold lower kinase activity in early mitosis than in interphase or in the early stages of postmitotic spreading. These findings suggest a model in which MLCK and the myosin II phosphatase (Totsukawa, G., Y. Yamakita, S. Yamashiro, H. Hosoya, D.J. Hartshorne, and F. Matsumura. 1999. J. Cell Biol. 144:735-744) act cooperatively to regulate the level of Ser 19-phosphorylated myosin II during mitosis and initiate cytokinesis through the activation of myosin II motor activity.

Indexed as

Cell CycleActinsActomyosinAmino Acid MotifsAmino Acid SequenceAnimalsBirdsCell DivisionCell LineHeLa CellsHumansInterphaseIsoenzymesModels, BiologicalMolecular Motor ProteinsMolecular WeightActinsActomyosinIsoenzymesMolecular Motor ProteinsMyosin-Light-Chain KinaseMyosin-Light-Chain PhosphataseMyosinsPhosphoprotein PhosphatasesPhosphoserineRecombinant Fusion Proteins

Identifiers

PMID11062269
PMCPMC2185581
OpenAlexW2169881041

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.