Evidence map›Paper›PMID 22274710›Full record

ReviewCell adhesion & migration

Central role of paxillin phosphorylation in regulation of LFA-1 integrins activity and lymphocyte migration.

Larisa Y Romanova, J Frederic Mushinski

Open access · goldAbstract readReview
In one paragraph

Review in Cell adhesion & migration. 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
0.2field-weighted citation impact, top 51% 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, 28 citations in OpenAlex.

  1. Article
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  8. Review
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  11. Interleukin-1Stem cells international · 2019
    Article
  12. Article
  13. Paxillin: a crossroad in pathological cell migration.Journal of hematology & oncology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Larisa Y RomanovaLaboratory of Cancer Biology and Genetics, National Cancer Institute, NIH, Bethesda, MD, USA. romanovl@mail.nih.gov
J Frederic Mushinski
National Cancer Institute · US

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

Coordinated changes of actin cytoskeleton and cell adhesion accompany maturation of lymphoid cells, their migration through lymphoid organs and to sites of inflammation, as well as metastasis of transformed cells. Here we discuss the central role of the actin-regulating adaptor protein, paxillin, during lymphocyte transition from a polarized, motile cell phenotype with partially active LFA-1 integrins to a round and immobile one with fully active LFA-1. In Baf3 murine pro-B lymphocytes, the former phenotype is induced by IL-3 that stimulates a FAK-mediated phosphorylation of paxillin at tyrosines (Y) 31 and 118 and a consequent Rac1 activation. Rearrangements of actin cytoskeleton that lead to the cell's acquisition of a spherical shape and LFA-1 activation are achieved upon activation of PKC-δ that binds and directly phosphorylates paxillin at threonine (T) 538 with consequent RhoA activation. This is accompanied by dephosphorylation of paxillin Y31/118 and by Rac1 inactivation. We propose a model of signaling cascades that reflects the interplay between the IL-3- and PKC-δ-mediated pathways.

Indexed as

Cell MovementProtein Processing, Post-TranslationalActin CytoskeletonAnimalsHumansLymphocyte Function-Associated Antigen-1LymphocytesPaxillinPhosphorylationProtein Kinase C-deltaProtein MultimerizationSignal TransductionLymphocyte Function-Associated Antigen-1PaxillinProtein Kinase C-delta

Identifiers

PMID22274710
PMCPMC3277778
OpenAlexW1967714882

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.