Evidence map›Paper›PMID 22869380›Full record

ArticleThe Journal of biological chemistry2012

Structural basis for paxillin binding and focal adhesion targeting of β-parvin.

Amy L Stiegler, Kyle M Draheim, Xiaofeng Li, Naomi E Chayen, David A Calderwood, Titus J Boggon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 38 citations in OpenAlex.

  1. 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 · 2026
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  14. Chapter 22: Structural and signaling functions of integrins.Biochimica et biophysica acta. Biomembranes · 2020
    Review
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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

6 authors at 3 institutions in 2 countries.

Amy L StieglerDepartment of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Kyle M Draheim
Xiaofeng Li
Naomi E Chayen
David A Calderwood
Titus J Boggon
Yale Cancer Center · USYale University · USImperial College London · GB

Funding

Structure and function of the integrin-linked kinase-PINCH-parvin complexR01GM088240 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2009 to 2012
$1.4M
Biacore T100 SPR system for studying and characterizing biomolecular interactionS10RR026992 · NCRR · YALE UNIVERSITY · PI FOLTA-STOGNIEW, EWA JOANNA · 2009 to 2009
$364k
NCRR NIH HHS RR026992NCRR NIH HHS S10 RR026992NIGMS NIH HHS R01 GM088240NIGMS NIH HHS R01GM088240
6 · The paper itself

Abstract

β-Parvin is a cytoplasmic adaptor protein that localizes to focal adhesions where it interacts with integrin-linked kinase and is involved in linking integrin receptors to the cytoskeleton. It has been reported that despite high sequence similarity to α-parvin, β-parvin does not bind paxillin, suggesting distinct interactions and cellular functions for these two closely related parvins. Here, we reveal that β-parvin binds directly and specifically to leucine-aspartic acid repeat (LD) motifs in paxillin via its C-terminal calponin homology (CH2) domain. We present the co-crystal structure of β-parvin CH2 domain in complex with paxillin LD1 motif to 2.9 Å resolution and find that the interaction is similar to that previously observed between α-parvin and paxillin LD1. We also present crystal structures of unbound β-parvin CH2 domain at 2.1 Å and 2.0 Å resolution that show significant conformational flexibility in the N-terminal α-helix, suggesting an induced fit upon paxillin binding. We find that β-parvin has specificity for the LD1, LD2, and LD4 motifs of paxillin, with K(D) values determined to 27, 42, and 73 μM, respectively, by surface plasmon resonance. Furthermore, we show that proper localization of β-parvin to focal adhesions requires both the paxillin and integrin-linked kinase binding sites and that paxillin is important for early targeting of β-parvin. These studies provide the first molecular details of β-parvin binding to paxillin and help define the requirements for β-parvin localization to focal adhesions.

Indexed as

ActininAmino Acid MotifsCrystallography, X-RayFocal AdhesionsHumansPaxillinProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryRepetitive Sequences, Amino AcidSurface Plasmon ResonanceActininPARVB protein, humanPaxillinPXN protein, human

Identifiers

PMID22869380
PMCPMC3463362
OpenAlexW2102801515

What OpenQuestion holds

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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.