Evidence map›Paper›PMID 10477763›Full record

ArticleThe Journal of cell biology1999

Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells.

D A Cheresh, J Leng, R L Klemke

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
9.6field-weighted citation impact, top 1% 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

91 citing papers in PubMed, 256 citations in OpenAlex.

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  12. The nanomorphology of cell surfaces of adhered osteoblasts.Beilstein journal of nanotechnology · 2021
    Article
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  20. Proteasome proteolysis supports stimulated platelet function and thrombosis.Arteriosclerosis, thrombosis, and vascular biology · 2014
    Article

31 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

D A ChereshDepartments of Immunology and Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
J Leng
R L Klemke
Scripps Research Institute · US

Funding

VEGF and PDGF in angiogenesis and tumor progressionR37CA050286 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1999 to 2013
$6.3M
STRUCTURAL AND FUNCTIONAL STUDIES--INTEGERIN-DEPENDENTR01CA050286 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1989 to 2018
$1.9M
SIGNALING MECHANISMS OF CELL MOTILITY &TUMOR METASTASISR29CA078493 · NCI · SCRIPPS RESEARCH INSTITUTE · PI KLEMKE, RICHARD L. · 1998 to 2002
$495k
NCI NIH HHS CA 45728NCI NIH HHS CA 50286NCI NIH HHS CA 78493-01NCI NIH HHS R01 CA050286NCI NIH HHS R37 CA050286
6 · The paper itself

Abstract

Cell migration and wound contraction requires assembly of actin into a functional myosin motor unit capable of generating force. However, cell migration also involves formation of actin-containing membrane ruffles. Evidence is provided that actin-myosin assembly and membrane ruffling are regulated by distinct signaling pathways in the migratory cell. Interaction of cells with extracellular matrix proteins or cytokines promote cell migration through activation of the MAP kinases ERK1 and ERK2 as well as the molecular coupling of the adaptor proteins p130CAS and c-CrkII. ERK signaling is independent of CAS/Crk coupling and regulates myosin light chain phosphorylation leading to actin-myosin assembly during cell migration and cell-mediated contraction of a collagen matrix. In contrast, membrane ruffling, but not cell contraction, requires Rac GTPase activity and the formation of a CAS/Crk complex that functions in the context of the Rac activating protein DOCK180. Thus, during cell migration ERK and CAS/Crk coupling operate as components of distinct signaling pathways that control actin assembly into myosin motors and membrane ruffles, respectively.

Indexed as

Cell MovementProto-Oncogene ProteinsSignal TransductionActinsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCell AdhesionCell MembraneCell SizeCOS CellsExtracellular Matrix ProteinsGTP-Binding ProteinsInsulinMitogen-Activated Protein Kinase KinasesMolecular Motor ProteinsMyosin-Light-Chain KinaseActinsCalcium-Calmodulin-Dependent Protein KinasesDOCK1 protein, humanExtracellular Matrix ProteinsGTP-Binding ProteinsInsulinMitogen-Activated Protein Kinase KinasesMolecular Motor ProteinsMyosin-Light-Chain KinaseMyosin Light ChainsMyosinsPhosphoproteinsProtein KinasesProteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-crkrac GTP-Binding ProteinsRetinoblastoma-Like Protein p130

Identifiers

PMID10477763
PMCPMC2169492
OpenAlexW2170503323

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.