Evidence map›Paper›PMID 9837942›Full record

ArticleThe Journal of biological chemistry1998

Cytoskeletal interactions with the leukocyte integrin beta2 cytoplasmic tail. Activation-dependent regulation of associations with talin and alpha-actinin.

R Sampath, P J Gallagher, F M Pavalko

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 218 citations in OpenAlex.

  1. Review
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  3. Article
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  5. Review
  6. Article
  7. Frontiers in immunology · 2020
    Review
  8. Article
  9. Novel functions of CCM1 delimit the relationship of PTB/PH domains.Biochimica et biophysica acta. Proteins and proteomics · 2017
    Article
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  11. Article
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  13. Review
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  20. Review

1 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 2 institutions in 1 country.

R SampathDepartment of Physiology and Biophysics, Indiana University School of Medicine, Indianapolis, Indiana 46202-5120, USA.
P J Gallagher
F M Pavalko
Indiana University – Purdue University Indianapolis · USIndiana University School of Medicine

Funding

Regulation of Apoptosis by DAPKR01HL054118 · NHLBI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI GALLAGHER, PATRICIA J · 1997 to 2006
$1.6M
CYTOSKELETAL-INTEGRIN INTERACTIONS IN NEUTROPHILSR55GM047333 · NIGMS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI PAVALKO, FREDRICK M · 1994 to 1994
–
NHLBI NIH HHS HL54118NHLBI NIH HHS R01 HL054118NIGMS NIH HHS GM47333
6 · The paper itself

Abstract

Circulating leukocytes are nonadherent but bind tightly to endothelial cells following activation. The increased avidity of leukocyte integrins for endothelial ligands following activation is regulated, in part, by interaction of the beta2 subunit cytoplasmic tail with the actin cytoskeleton. We propose a mechanism to explain how tethering of the actin cytoskeleton to leukocyte integrins is regulated. In resting leukocytes, beta2 integrins are constitutively linked to the actin cytoskeleton via the protein talin. Activation of cells induces proteolysis of talin and dissociation from the beta2 tail. This phase is transient, however, and is followed by reattachment of actin filaments to integrins that is mediated by the protein alpha-actinin. The association of alpha-actinin with integrins may stabilize the cytoskeleton and promote firm adhesion to and migration across the endothelium. Glutathione S-transferase-beta2 tail fusion protein/mutagenesis experiments suggest that the affinity of alpha-actinin binding to the beta2 tail is regulated by a change in the conformation of the tail that unmasks a cryptic alpha-actinin binding domain. Positive and inhibitory domains within the beta2 tail regulate alpha-actinin binding: a single 11-amino acid region (residues 736-746) is necessary and sufficient for alpha-actinin binding, and a regulatory domain between residues 748-762 inhibits constitutive association of the beta2 tail with alpha-actinin.

Indexed as

ActininAmino Acid SequenceCD18 AntigensCell AdhesionCell MovementCytoskeletonGlutathione TransferaseHumansMolecular Sequence DataNeutrophil ActivationNeutrophilsProtein BindingRecombinant Fusion ProteinsTalinActininCD18 AntigensGlutathione TransferaseRecombinant Fusion ProteinsTalin

Identifiers

PMID9837942
PMCPMC2823626
OpenAlexW2048127037

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.