Evidence map›Paper›PMID 12952069›Full record

ReviewJournal of muscle research and cell motility2002

Signaling pathways regulating Dictyostelium myosin II.

Marc A De la Roche, Janet L Smith, Venkaiah Betapudi, Thomas T Egelhoff, Graham P Côté

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. SuggestingCells · 2024
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  7. A Cdc42- and Rac-interactive binding (CRIB) domain mediates functions of coronin.Proceedings of the National Academy of Sciences of the United States of America · 2014
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  16. The alpha-kinase family: an exceptional branch on the protein kinase tree.Cellular and molecular life sciences : CMLS · 2010
    Review
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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 3 institutions in 2 countries.

Marc A De la RocheDepartment of Biochemistry, Botterell Hall, Queen's University, Kingston, Ontario, Canada K7L 3N6.
Janet L Smith
Venkaiah Betapudi
Thomas T Egelhoff
Graham P Côté
Case Western Reserve University · USQueen's University · CABoston Biomedical Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dictyostelium myosin II is a conventional, two-headed myosin that consists of two copies each of a myosin heavy chain (MHC), an essential light chain (ELC) and a regulatory light chain (RLC). The MHC is comprised of an amino-terminal motor domain, a neck region that binds the RLC and ELC and a carboxyl-terminal alpha-helical coiled-coil tail. Electrostatic interactions between the tail domains mediate the self-assembly of myosin II into bipolar filaments that are capable of interacting with actin filaments to generate a contractile force. In this review we discuss the regulation of Dictyostelium myosin II by a myosin light chain kinase (MLCK-A) that phosphorylates the RLC and increases motor activity and by MHC kinases (MHCKs) that phosphorylate the tail and prevent filament assembly. Dictyostelium may express as many as four MHCKs (MHCK A-D) consisting of an atypical alpha-kinase catalytic domain and a carboxyl-terminal WD repeat domain that targets myosin II filaments. A previously reported MHCK, termed MHC-PKC, now seems more likely to be a diacylglycerol kinase (DgkA). The relationship of the MHCKs to the larger family of alpha-kinases is discussed and key features of the structure of the alpha-kinase catalytic domain are reviewed. Potential upstream regulators of myosin II are described, including DgkA, cGMP, cAMP and PAKa, a target for Rac GTPases. Recent results point to a complex network of signaling pathways responsible for controling the activity and localization of myosin II in the cell.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCalcium-Calmodulin-Dependent Protein KinasesDictyosteliumModels, MolecularMyosin Light ChainsMyosin Type IIProtein ConformationProtozoan ProteinsSignal TransductionCalcium-Calmodulin-Dependent Protein Kinasesmyosin-heavy-chain kinaseMyosin Light ChainsMyosin Type IIProtozoan Proteins

Identifiers

PMID12952069
OpenAlexW1594501126

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.