Evidence map›Paper›PMID 7806572›Full record

ArticleThe Journal of cell biology1994

Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells.

B D Ostrow, P Chen, R L Chisholm

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.7field-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

35 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  4. Various Themes of Myosin Regulation.Journal of molecular biology · 2016
    Review
  5. Review
  6. Nonmuscle myosin-2: mix and match.Cellular and molecular life sciences : CMLS · 2013
    Review
  7. Cytokinesis mechanics and mechanosensing.Cytoskeleton (Hoboken, N.J.) · 2012
    Review
  8. Cytokinesis through biochemical-mechanical feedback loops.Seminars in cell & developmental biology · 2010
    Review
  9. Article
  10. Article
  11. Article
  12. Mechanics and regulation of cytokinesis.Current opinion in cell biology · 2004
    Review
  13. Article
  14. Article
  15. Article
  16. Parameters that specify the timing of cytokinesis.The Journal of cell biology · 1999
    Article
  17. Article
  18. Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  19. MLCK-A, an unconventional myosin light chain kinase from Dictyostelium, is activated by a cGMP-dependent pathway.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

B D OstrowDepartment of Cell, Molecular, and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
P Chen
R L Chisholm
Northwestern University · US

Funding

MOLECULAR GENETIC ANALYSIS OF MOTILITY: MYOSIN LCSR01GM039264 · NIGMS · NORTHWESTERN UNIVERSITY · PI CHISHOLM, REX L · 1988 to 2002
$1.0M
NIGMS NIH HHS GM39264
6 · The paper itself

Abstract

In a number of systems phosphorylation of the regulatory light chain (RMLC) of myosin regulates the activity of myosin. In smooth muscle and vertebrate nonmuscle systems RMLC phosphorylation is required for contractile activity. In Dictyostelium discoideum phosphorylation of the RMLC regulates both ATPase activity and motor function. We have determined the site of phosphorylation on the Dictyostelium RMLC and used site-directed mutagenesis to replace the phosphorylated serine with an alanine. The mutant light chain was then expressed in RMLC null Dictyostelium cells (mLCR-) from an actin promoter on an integrating vector. The mutant RMLC was expressed at high levels and associated with the myosin heavy chain. RMLC bearing a ser13ala substitution was not phosphorylated in vitro by purified myosin light chain kinase, nor could phosphate be detected on the mutant RMLC in vivo. The mutant myosin had reduced actin-activated ATPase activity, comparable to fully dephosphorylated myosin. Unexpectedly, expression of the mutant RMLC rescued the primary phenotypic defects of the mlcR- cells to the same extent as did expression of wild-type RMLC. These results suggest that while phosphorylation of the Dictyostelium RMLC appears to be tightly regulated in vivo, it is not essential for myosin-dependent cellular functions.

Indexed as

MutationActinsAdenosine TriphosphatasesAmino Acid SequenceAnimalsBase SequenceCell CompartmentationCell DivisionDictyosteliumEnzyme ActivationFluorescent Antibody TechniqueGenetic Complementation TestMolecular Sequence DataMutagenesis, Site-DirectedMyosin-Light-Chain KinaseMyosinsActinsAdenosine TriphosphatasesMyosin-Light-Chain KinaseMyosinsRecombinant ProteinsSerine

Identifiers

PMID7806572
PMCPMC2120314
OpenAlexW2111998377

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.