Evidence map›Paper›PMID 17473008›Full record

ArticleProtein science : a publication of the Protein Society2007

Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.

Clare J McCleverty, Diane C Lin, Robert C Liddington

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 80 citations in OpenAlex.

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  17. EphA2 signaling within integrin adhesions regulates fibrillar adhesion elongation and fibronectin deposition.Matrix biology : journal of the International Society for Matrix Biology · 2021
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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

3 authors at 2 institutions in 1 country.

Clare J McClevertyCancer Center, Burnham Institute for Medical Research, La Jolla, California 92037, USA.
Diane C Lin
Robert C Liddington
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of California, Irvine · US

Funding

CYTOCHALASINS, ACTIN FILAMENTS, AND CELL MOTILITYR01GM022289 · NIGMS · UNIVERSITY OF CALIFORNIA IRVINE · PI LIN, SHIN · 1985 to 1999
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NIGMS NIH HHS GM22289
6 · The paper itself

Abstract

Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell-matrix adhesion. Here we describe the crystal structure of the phosphotyrosine-binding (PTB) domain of tensin1, and show that it binds integrins in an NPxY-dependent fashion. Alanine mutagenesis of both the PTB domain and integrin tails supports a model of integrin binding similar to that of the PTB-like domain of talin. However, we also show that phosphorylation of the NPxY tyrosine, which disrupts talin binding, has a negligible effect on tensin binding. This suggests that tyrosine phosphorylation of integrin, which occurs during the maturation of focal adhesions, could act as a switch to promote the migration of tensin-integrin complexes into fibronectin-mediated fibrillar adhesions.

Indexed as

Amino Acid SequenceAnimalsChickensCrystallography, X-RayIntegrinsMicrofilament ProteinsMolecular Sequence DataPhosphorylationPhosphotyrosineProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidTalinTensinsTyrosineIntegrinsMicrofilament ProteinsPhosphotyrosineTalinTensinsTyrosine

Identifiers

PMID17473008
PMCPMC2206669
OpenAlexW2102674665

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.