ArticleStructure (London, England : 1993)2019
Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion.
Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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.
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.
Who cites it
32 citing papers in PubMed, 45 citations in OpenAlex.
- Functional genomic screens uncover FERMT2 as a critical regulator of YAP/TAZ-driven tumorigenicity.Cell death and differentiation · 2026Article
- ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Synergistic effect of PIPBiophysical journal · 2026Article
- Paxillin mediates ARP2-dependent actin assembly for spindle migration in mammalian oocyte meiosis.Biology direct · 2026Article
- Force Transmission by Minimal Focal Adhesion Complexes Induces Synthetic Cell Deformation.ACS synthetic biology · 2026Article
- Development of three-colour FRET cascade for force sensing of the putative RIAM-vinculin interaction in fibroblasts.Communications chemistry · 2025Article
- Mammalian cells measure the extracellular matrix area and respond through switching the adhesion state.Nature communications · 2025Article
- Mechanisms and consequences of myeloid adhesome dysfunction in atherogenesis.Cardiovascular research · 2025Article
- A flexible loop in the paxillin LIM3 domain mediates its direct binding to integrin β subunits.PLoS biology · 2024Article
- Surface-induced phase separation of reconstituted nascent integrin clusters on lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- ConFERMing the role of talin in integrin activation and mechanosignaling.Journal of cell science · 2023Article
- Structure, signal transduction, activation, and inhibition of integrin αIIbβ3.Thrombosis journal · 2023Review
- Opposite roles of Kindlin orthologs in cell survival and proliferation.Cell proliferation · 2022Article
- Bottom-up reconstitution of focal adhesion complexes.The FEBS journal · 2022Review
- Review
- Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022Review
- Mechanism of integrin activation by talin and its cooperation with kindlin.Nature communications · 2022Article
- Synergistic phase separation of two pathways promotes integrin clustering and nascent adhesion formation.eLife · 2022Article
- Paxillin: A Hub for Mechano-Transduction from the β3 Integrin-Talin-Kindlin Axis.Frontiers in cell and developmental biology · 2022Review
- Integrin-Mediated Tumorigenesis and Its Therapeutic Applications.Frontiers in oncology · 2022Review
Corrections and comments
- Commented on by
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Activation of cell surface receptor integrin has been extensively studied as the first key step to trigger cell adhesion, but the subsequent events, widely regarded as integrin "outside-in" signaling to form supramolecular complexes (focal adhesions [FAs]) to promote dynamic cell adhesion, remain poorly elucidated. Integrin activator kindlin-2 was recently found to associate with paxillin in nascent FAs, implicating an early yet undefined integrin outside-in signaling event. Here we show structurally that kindlin-2 recognizes paxillin via a distinct interface involving the ubiquitin-like kindlin-2 F0 domain and the paxillin LIM4 domain. The interface is adjacent to the membrane binding site of kindlin-2 F0, suggesting a mechanism for kindlin-2 to recruit paxillin to the membrane-proximal site where FA assembly is initiated. Disruption of the interface impaired the localization of paxillin, causing strong defects in FA assembly and cell migration. These data unveil a structural basis of the kindlin-2/paxillin interaction in controlling dynamic cell adhesion.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.