Evidence map›Paper›PMID 36231001›Full record

ReviewCells2022

Structural Basis of β2 Integrin Inside-Out Activation.

Lai Wen, Qingkang Lyu, Klaus Ley, Benjamin T Goult

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. INTEGRIN FUNCTION IN LEUKOCYTE-MEDIATED INFLAMMATION-ACTINOPATHIES IN IMMUNE DISEASES.Transactions of the American Clinical and Climatological Association · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Targeting Neutrophil βBiomolecules · 2023
    Review
  9. Review
  10. Article
  11. Structural biology of complement receptors.Frontiers in immunology · 2023
    Review
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

4 authors at 2 institutions in 2 countries.

Lai WenDepartment of Pharmacology, Center for Molecular and Cellular Signaling in the Cardiovascular System, Reno School of Medicine, University of Nevada, Reno, NV 89577, USA.
Qingkang LyuCenter for Autoimmunity and Inflammation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.
Klaus LeyCenter for Autoimmunity and Inflammation, La Jolla Institute for Immunology, La Jolla, CA 92037, USA.ORCID 0000-0001-9339-3672
Benjamin T GoultSchool of Biosciences, University of Kent, Canterbury CT2 7NJ, UK.ORCID 0000-0002-3438-2807
La Jolla Institute for Immunology · USUniversity of Kent · GB

Funding

Transgenic Animal Genotyping and Phenotyping CoreP20GM130459 · NIGMS · UNIVERSITY OF NEVADA RENO · PI Nathan Grainger · 2019 to 2026
$20.3M
The Hemostasis, Thrombosis, and Inflammation Models CoreP01HL151433 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Mark HOWARD Ginsberg · 2020 to 2026
$16.4M
Biotechnology and Biological Sciences Research Council BB/S007245/1Cancer Research UK CRUK-A21671NHLBI NIH HHS P01 HL151433NIGMS NIH HHS P20 GM130459
6 · The paper itself

Abstract

β2 integrins are expressed on all leukocytes. Precise regulation of the β2 integrin is critical for leukocyte adhesion and trafficking. In neutrophils, β2 integrins participate in slow rolling. When activated by inside-out signaling, fully activated β2 integrins mediate rapid leukocyte arrest and adhesion. The two activation pathways, starting with selectin ligand engagement and chemokine receptor ligation, respectively, converge on phosphoinositide 3-kinase, talin-1, kindlin-3 and Rap1. Here, we focus on recent structural insights into autoinhibited talin-1 and autoinhibited trimeric kindlin-3. When activated, both talin-1 and kindlin-3 can bind the β2 cytoplasmic tail at separate but adjacent sites. We discuss possible pathways for talin-1 and kindlin-3 activation, recruitment to the plasma membrane, and their role in integrin activation. We propose new models of the final steps of integrin activation involving the complex of talin-1, kindlin-3, integrin and the plasma membrane.

Indexed as

CD18 AntigensTalinIntegrinsLigandsPhosphatidylinositol 3-KinasePhosphatidylinositol 3-KinasesReceptors, ChemokineSelectinsCD18 AntigensIntegrinsLigandsPhosphatidylinositol 3-KinasePhosphatidylinositol 3-KinasesReceptors, ChemokineSelectinsTalinactivationcell adhesionchemokineintegrinkindlinleukocytesneutrophilsRap1structural biologytalin

Identifiers

PMID36231001
PMCPMC9564206
OpenAlexW4297464547

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.