Evidence map›Paper›PMID 18799623›Full record

ArticleMolecular biology of the cell2008

Rap1 activation in collagen phagocytosis is dependent on nonmuscle myosin II-A.

Pamela D Arora, Mary Anne Conti, Shoshana Ravid, David B Sacks, Andras Kapus, Robert S Adelstein, Anne R Bresnick, Christopher A McCulloch

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. [Research progression of the relationship between integrin α2β1 and drug-induced gingival overgrowth].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Focal adhesions and Ras are functionally and spatially integrated to mediate IL-1 activation of ERK.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  11. Article
  12. Review
  13. 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

8 authors at 5 institutions in 2 countries.

Pamela D AroraCIHR Group in Matrix Dynamics, University of Toronto, Toronto, ON M5S 3E2, Canada.
Mary Anne Conti
Shoshana Ravid
David B Sacks
Andras Kapus
Robert S Adelstein
Anne R Bresnick
Christopher A McCulloch
National Institutes of Health · USUniversity of Toronto · CAAlbert Einstein College of Medicine · USBrigham and Women's Hospital · USSt. Michael's Hospital · CA

Funding

In Vivo Function of Nonmuscle Myosin II-AZIAHL004218 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 2009 to 2019
$5.1M
In Vivo Function of Nonmuscle Myosin II-AZ01HL004218 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ADELSTEIN, ROBERT · 1991 to 2008
$826k
6 · The paper itself

Abstract

Rap1 enhances integrin-mediated adhesion but the link between Rap1 activation and integrin function in collagen phagocytosis is not defined. Mass spectrometry of Rap1 immunoprecipitates showed that the association of Rap1 with nonmuscle myosin heavy-chain II-A (NMHC II-A) was enhanced by cell attachment to collagen beads. Rap1 colocalized with NM II-A at collagen bead-binding sites. There was a transient increase in myosin light-chain phosphorylation after collagen-bead binding that was dependent on myosin light-chain kinase but not Rho kinase. Inhibition of myosin light-chain phosphorylation, but not myosin II-A motor activity inhibited collagen-bead binding and Rap activation. In vitro binding assays demonstrated binding of Rap1A to filamentous myosin rods, and in situ staining of permeabilized cells showed that NM II-A filaments colocalized with F-actin at collagen bead sites. Knockdown of NM II-A did not affect talin, actin, or beta1-integrin targeting to collagen beads but targeting of Rap1 and vinculin to collagen was inhibited. Conversely, knockdown of Rap1 did not affect localization of NM II-A to beads. We conclude that MLC phosphorylation in response to initial collagen-bead binding promotes NM II-A filament assembly; binding of Rap1 to myosin filaments enables Rap1-dependent integrin activation and enhanced collagen phagocytosis.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsCollagenEnzyme ActivationFibroblastsHeterocyclic Compounds, 4 or More RingsHumansIntegrin beta1MiceMolecular Sequence DataMyosin-Light-Chain KinaseNonmuscle Myosin Type IIAPeptidesPhagocytosisrap1 GTP-Binding ProteinsblebbistatinCollagenHeterocyclic Compounds, 4 or More RingsIntegrin beta1Myosin-Light-Chain KinaseNonmuscle Myosin Type IIAPeptidesrap1 GTP-Binding ProteinsRecombinant Fusion ProteinsRNA, Small InterferingTalin

Identifiers

PMID18799623
PMCPMC2592653
OpenAlexW2050119726

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.