Evidence map›Paper›PMID 9636140›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix.

B E Slack

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 62 citations in OpenAlex.

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  2. CBFrontiers in cellular neuroscience · 2020
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  16. Myelin proteolipid protein forms a complex with integrins and may participate in integrin receptor signaling in oligodendrocytes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
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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

1 author at 1 institution in 1 country.

B E SlackDepartment of Pathology and Laboratory Medicine, Boston University School of Medicine, Boston MA 02118, USA. bslack@bu.edu
Boston University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The G protein-coupled m1 and m3 muscarinic acetylcholine receptors increase tyrosine phosphorylation of several proteins, including the focal adhesion-associated proteins paxillin and focal adhesion kinase (FAK), but the mechanism is not understood. Activation of integrins during adhesion of cells to extracellular matrix, or stimulation of quiescent cell monolayers with G protein-coupled receptor ligands including bradykinin, bombesin, endothelin, vasopressin, and lysophosphatidic acid, also induces tyrosine phosphorylation of paxillin and FAK and formation of focal adhesions. These effects are generally independent of protein kinase C but are inhibited by agents that prevent cytoskeletal assembly or block activation of the small molecular weight G protein Rho. This report demonstrates that tyrosine phosphorylation of paxillin and FAK elicited by stimulation of muscarinic m3 receptors with the acetylcholine analog carbachol is inhibited by soluble peptides containing the arginine-glycine-aspartate motif (the recognition site for integrins found in adhesion proteins such as fibronectin) but is unaffected by peptides containing the inactive sequence arginine-glycine-glutamate. Tyrosine phosphorylation elicited by carbachol, but not by cell adhesion to fibronectin, is reduced by the protein kinase C inhibitor GF 109203X. The response to carbachol is dependent on the presence of fibronectin. Moreover, immunofluorescence studies show that carbachol treatment induces formation of stress fibers and focal adhesions. These results suggest that muscarinic receptor stimulation activates integrins via a protein kinase C-dependent mechanism. The activated integrins transmit a signal into the cell's interior leading to tyrosine phosphorylation of paxillin and FAK. This represents a novel mechanism for regulation of tyrosine phosphorylation by muscarinic receptors.

Indexed as

Cell AdhesionCell Adhesion MoleculesCells, CulturedCytoskeletal ProteinsExtracellular MatrixFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrinsPaxillinPhosphoproteinsPhosphorylationProtein Kinase CProtein-Tyrosine KinasesReceptor, Muscarinic M3Receptors, MuscarinicCell Adhesion MoleculesCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesIntegrinsPaxillinPhosphoproteinsProtein Kinase CProtein-Tyrosine KinasesPTK2 protein, humanPXN protein, humanReceptor, Muscarinic M3Receptors, MuscarinicTyrosine

Identifiers

PMID9636140
PMCPMC22590
OpenAlexW1963754791

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.