Evidence map›Paper›PMID 21316371›Full record

ArticleJournal of molecular biology2011

A proteomic study of myosin II motor proteins during tumor cell migration.

Venkaiah Betapudi, Giridharan Gokulrangan, Mark R Chance, Thomas T Egelhoff

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

27 citing papers in PubMed, 39 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Role of motor proteins in human cancers.Saudi journal of biological sciences · 2022
    Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Pharmacological activation of myosin II paralogs to correct cell mechanics defects.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

4 authors at 2 institutions in 1 country.

Venkaiah BetapudiDepartment of Cell Biology, Lerner College of Medicine, Case Western Reserve University, The Lerner Research Institute, Cleveland Clinic Foundation, 9500 Euclid Avenue, Cleveland, OH 44195, USA.
Giridharan Gokulrangan
Mark R Chance
Thomas T Egelhoff
Case Western Reserve University · USCleveland Clinic Lerner College of Medicine · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MARK R CHANCE · 1987 to 2026
$142.3M
Myosin Assembly in DictyosteliumR01GM050009 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI EGELHOFF, THOMAS · 1998 to 2017
$4.7M
Myosin II Dynamics and Assembly in Mammalian CellsR01GM077224 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI EGELHOFF, THOMAS · 2007 to 2010
$1.1M
NCI NIH HHS P30 CA043703NCI NIH HHS P30-CA-043703NIGMS NIH HHS GM077224NIGMS NIH HHS R01 GM050009NIGMS NIH HHS R01 GM077224
6 · The paper itself

Abstract

Myosin II motor proteins play important roles in cell migration. Although myosin II filament assembly plays a key role in the stabilization of focal contacts at the leading edge of migrating cells, the mechanisms and signaling pathways regulating the localized assembly of lamellipodial myosin II filaments are poorly understood. We performed a proteomic analysis of myosin heavy chain (MHC) phosphorylation sites in MDA-MB 231 breast cancer cells to identify MHC phosphorylation sites that are activated during integrin engagement and lamellar extension on fibronectin. Fibronectin-activated MHC phosphorylation was identified on novel and previously recognized consensus sites for phosphorylation by protein kinase C and casein kinase II (CK-II). S1943, a CK-II consensus site, was highly phosphorylated in response to matrix engagement, and phosphoantibody staining revealed phosphorylation on myosin II assembled into leading-edge lamellae. Surprisingly, neither pharmacological reduction nor small inhibitory RNA reduction in CK-II activity reduced this stimulated S1943 phosphorylation. Our data demonstrate that S1943 phosphorylation is upregulated during lamellar protrusion, and that CK-II does not appear to be the kinase responsible for this matrix-induced phosphorylation event.

Indexed as

AnimalsBreast NeoplasmsCasein Kinase IICell Line, TumorCell MovementChlorocebus aethiopsCOS CellsFemaleFibronectinsHeLa CellsHumansModels, MolecularMyosin Heavy ChainsMyosin Type IIPhosphorylationProtein IsoformsCasein Kinase IIFibronectinsMyosin Heavy ChainsMyosin Type IIProtein IsoformsProteomeRecombinant Fusion ProteinsRNA, Small Interfering

Identifiers

PMID21316371
PMCPMC3072708
OpenAlexW2043273198

What OpenQuestion holds

Textmetadata
LicenceTDM
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.