Evidence map›Paper›PMID 9037011›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I.

H Brzeska, U G Knaus, Z Y Wang, G M Bokoch, E D Korn

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023
    Article
  3. Review
  4. Review
  5. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  6. Various Themes of Myosin Regulation.Journal of molecular biology · 2016
    Review
  7. Components of the CtBP1/BARS-dependent fission machinery.Histochemistry and cell biology · 2013
    Review
  8. Article
  9. Potential roles of myosin VI in cell motility.Biochemical Society transactions · 2009
    Review
  10. How are the cellular functions of myosin VI regulated within the cell?Biochemical and biophysical research communications · 2008
    Review
  11. p21-activated kinase signaling in breast cancer.Breast cancer research : BCR · 2005
    Review
  12. Myosin VI: cellular functions and motor properties.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Myosin I heavy chain kinase: cloning of the full-length gene and acidic lipid-dependent activation by Rac and Cdc42.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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 1 institution in 1 country.

H BrzeskaLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892-0301, USA.
U G Knaus
Z Y Wang
G M Bokoch
E D Korn
National Heart Lung and Blood Institute · US

Funding

REGULATION OF NEUTROPHIL RECEPTOR/G PROTEIN INTERACTIONSR01GM039434 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DERMARDIROSSIAN, CELINE · 1988 to 2009
$4.7M
NIGMS NIH HHS GM39434NIGMS NIH HHS R01 GM039434
6 · The paper itself

Abstract

Acanthamoeba class I myosins are unconventional, single-headed myosins that express actin-activated Mg2+-ATPase and in vitro motility activities only when a single serine or threonine in the heavy chain is phosphorylated by myosin I heavy chain kinase (MIHCK). Some other, but not most, class I myosins have the same consensus phosphorylation site sequence, and the two known class VI myosins have a phosphorylatable residue in the homologous position, where most myosins have an aspartate or glutamate residue. Recently, we found that the catalytic domain of Acanthamoeba MIHCK has extensive sequence similarity to the p21-activated kinase (PAK)/STE20 family of kinases from mammals and yeast, which are activated by small GTP-binding proteins. The physiological substrates of the PAK/STE20 kinases are not well characterized. In this paper we show that PAK1 has similar substrate specificity as MIHCK when assayed against synthetic substrates and that PAK1 phosphorylates the heavy chain (1 mol of P(i) per mol) and activates Acanthamoeba myosin I as MIHCK does. These results, together with the known involvement of Acanthamoeba myosin I, yeast myosin I, STE20, PAK, and small GTP-binding proteins in membrane- and cytoskeleton-associated morphogenetic transformations and activities, suggest that myosins may be physiological substrates for the PAK/STE20 family and thus mediators of these events.

Indexed as

AcanthamoebaAnimalsCalcium-Calmodulin-Dependent Protein KinasesEnzyme ActivationMyosinsPhosphorylationProtein Serine-Threonine KinasesProtozoan ProteinsSubstrate SpecificityCalcium-Calmodulin-Dependent Protein Kinasesmyosin-heavy-chain kinaseMyosinsProtein Serine-Threonine KinasesProtozoan Proteins

Identifiers

PMID9037011
PMCPMC19749
OpenAlexW2020277297

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.