Evidence map›Paper›PMID 22081014›Full record

ArticleNature structural & molecular biology2011

NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling.

Peter D Mace, Yann Wallez, Małgorzata K Dobaczewska, Jeongeun J Lee, Howard Robinson, Elena B Pasquale, Stefan J Riedl

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

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  12. A novel spontaneous mutation of BCAR3 results in extrusion cataracts in CF#1 mouse strain.Mammalian genome : official journal of the International Mammalian Genome Society · 2016
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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

7 authors at 3 institutions in 1 country.

Peter D MaceProgram of Apoptosis and Cell Death Research, Cancer Center, Sanford-Burnham Medical Research Institute, La Jolla, California, USA.
Yann Wallez
Małgorzata K Dobaczewska
Jeongeun J Lee
Howard Robinson
Elena B Pasquale
Stefan J Riedl
Sanford Burnham Prebys Medical Discovery Institute · USBrookhaven National Laboratory · USUniversity of California, San Diego · US

Funding

Tissue CultureP01HD025938 · NICHD · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STALLCUP, WILLIAM B. · 1989 to 2011
$13.6M
Signaling Interactions in Cell Survival and InvasionP01CA102583 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ELY, KATHRYN R. · 2004 to 2008
$11.4M
Structure and Function of BCAR1 and BCAR3 Association in Breast Cancer MalignancyR01CA160457 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B, RIEDL, STEFAN J · 2011 to 2015
$2.2M
The EphB4 Receptor as a Novel Breast Cancer TargetR01CA116099 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2006 to 2010
$1.9M
NCI NIH HHS P01 CA102583NCI NIH HHS P01CA102583NCI NIH HHS R01 CA116099NCI NIH HHS R01CA116099NCI NIH HHS R01 CA160457NCI NIH HHS R01CA160457NICHD NIH HHS P01 HD025938NICHD NIH HHS P01HD025938
6 · The paper itself

Abstract

Members of the novel SH2-containing protein (NSP) and Crk-associated substrate (Cas) protein families form multidomain signaling platforms that mediate cell migration and invasion through a collection of distinct signaling motifs. Members of each family interact via their respective C-terminal domains, but the mechanism of this association has remained enigmatic. Here we present the crystal structures of the C-terminal domain from the NSP protein BCAR3 and the complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but it has a 'closed' conformation incapable of enzymatic activity. The structure of the NSP3-p130Cas complex reveals that this closed conformation is instrumental for interaction of NSP proteins with a focal adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor conversion enables high-affinity, yet promiscuous, interactions between NSP and Cas proteins and represents an unprecedented mechanistic paradigm linking cellular signaling networks.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingBinding SitesConserved SequenceCrk-Associated Substrate ProteinGuanine Nucleotide Exchange FactorsHumansModels, MolecularProtein Structure, TertiaryAdaptor Proteins, Signal TransducingBCAR1 protein, humanBCAR3 protein, humanCrk-Associated Substrate ProteinGuanine Nucleotide Exchange FactorsSH2D3C protein, human

Identifiers

PMID22081014
PMCPMC3230775
OpenAlexW2138244187

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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.