Evidence map›Paper›PMID 31391572›Full record

ArticleScientific reports2019

Paxillin S273 Phosphorylation Regulates Adhesion Dynamics and Cell Migration through a Common Protein Complex with PAK1 and βPIX.

Abira Rajah, Colton G Boudreau, Alina Ilie, Tse-Luen Wee, Kaixi Tang, Aleksandar Z Borisov, John Orlowski, Claire M Brown

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  16. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
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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

8 authors at 2 institutions in 1 country.

Abira RajahDepartment of Physiology, McGill University, Montreal, Canada.
Colton G BoudreauDepartment of Physiology, McGill University, Montreal, Canada.
Alina IlieDepartment of Physiology, McGill University, Montreal, Canada.
Tse-Luen WeeDepartment of Physiology, McGill University, Montreal, Canada.
Kaixi TangDepartment of Physiology, McGill University, Montreal, Canada.
Aleksandar Z BorisovDepartment of Physiology, McGill University, Montreal, Canada.
John OrlowskiDepartment of Physiology, McGill University, Montreal, Canada.
Claire M BrownDepartment of Physiology, McGill University, Montreal, Canada. claire.brown@mcgill.ca.ORCID http://orcid.org/0000-0003-1622-663X
McGill University · CAMcGill University Health Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell migration is an important biological phenomenon involved in many homeostatic and aberrant physiological processes. Phosphorylation of the focal adhesion adaptor protein, paxillin, on serine 273 (S273) has been implicated as a key regulator of cell migration. Here, it is shown that phosphorylation on paxillin S273 leads to highly migratory cells with small dynamic adhesions. Adhesions at protrusive edges of the cell were more dynamic than adhesions at retracting edges. Temporal image correlation microscopy revealed that these dynamic adhesions undergo rapid binding of paxillin, PAK1 and βPIX. We identified membrane proximal adhesion subdomains in protrusive regions of the cell that show rapid protein binding that is dependent on paxillin S273 phosphorylation, PAK1 kinase activity and phosphatases. These dynamic adhesion subdomains corresponded to regions of the adhesion that also show co-binding of paxillin/PAK1 and paxillin/βPIX complexes. It is likely that parts of individual adhesions are more dynamic while others are less dynamic due to their association with the actin cytoskeleton. Variable adhesion and binding dynamics are regulated via differential paxillin S273 phosphorylation across the cell and within adhesions and are required for regulated cell migration. Dysregulation through phosphomutants, PAK1-KD or βPIX mutants resulted in large stable adhesions, long protein binding times and slow cell migration. Dysregulation through phosphomimics or PAK1-CA led to small dynamic adhesions and rapid cell migration reminiscent of highly migratory cancer cells. Thus, phosphorylation of paxillin S273 is a key regulator of cell migration through recruitment of βPIX and PAK1 to sites of adhesion.

Indexed as

Cell AdhesionCell MovementAnimalsCHO CellsCricetulusIntravital MicroscopyMicroscopy, FluorescenceMutationp21-Activated KinasesPaxillinPhosphorylationProtein BindingProtein DomainsRecombinant ProteinsRho Guanine Nucleotide Exchange FactorsSerineArhgef7 protein, mousep21-Activated KinasesPak1 protein, mousePaxillinRecombinant ProteinsRho Guanine Nucleotide Exchange FactorsSerine

Identifiers

PMID31391572
PMCPMC6686007
OpenAlexW2966064090

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.