Evidence map›Paper›PMID 22667988›Full record

ArticleACS chemical biology2012

Bipartite tetracysteine display reveals allosteric control of ligand-specific EGFR activation.

Rebecca A Scheck, Melissa A Lowder, Jacob S Appelbaum, Alanna Schepartz

Abstract read
In one paragraph

Article in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 65 citations in OpenAlex.

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  19. Rotamer-Restricted Fluorogenicity of the Bis-Arsenical ReAsH.Journal of the American Chemical 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

4 authors at 1 institution in 1 country.

Rebecca A ScheckDepartment of Chemistry, Yale University, 225 Prospect Street, New Haven, CT 06520-8107, USA.
Melissa A Lowder
Jacob S Appelbaum
Alanna Schepartz
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Surveying protein partnerships and assembly with bipartite tetracysteine displayR01GM083257 · NIGMS · YALE UNIVERSITY · PI SCHEPARTZ, ALANNA · 2008 to 2018
$3.2M
In vivo monitoring of EGF receptor dimerization and activationF32GM087092 · NIGMS · YALE UNIVERSITY · PI SCHECK, REBECCA · 2009 to 2011
$144k
NIGMS NIH HHS 5 F32 GM087092-03NIGMS NIH HHS 5 R01 GM083257NIGMS NIH HHS F32 GM087092NIGMS NIH HHS R01 GM083257NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Aberrant activation of the epidermal growth factor receptor (EGFR), a prototypic receptor tyrosine kinase, is critical to the biology of many common cancers. The molecular events that define how EGFR transmits an extracellular ligand binding event through the membrane are not understood. Here we use a chemical tool, bipartite tetracysteine display, to report on ligand-specific conformational changes that link ligand binding and kinase activation for full-length EGFR on the mammalian cell surface. We discover that EGF binding is communicated to the cytosol through formation of an antiparallel coiled coil within the intracellular juxtamembrane (JM) domain. This conformational transition is functionally coupled to receptor activation by EGF. In contrast, TGFα binding is communicated to the cytosol through formation of a discrete, alternative helical interface. These findings suggest that the JM region can differentially decode extracellular signals and transmit them to the cell interior. Our results provide new insight into how EGFR communicates ligand-specific information across the membrane.

Indexed as

Allosteric SiteAnimalsBinding SitesBiochemistryCell MembraneCHO CellsCricetinaeCysteineDimerizationEpidermal Growth FactorErbB ReceptorsHumansLigandsProtein BindingProtein Structure, TertiaryTransforming Growth Factor alphaCysteineEpidermal Growth FactorErbB ReceptorsLigandsTransforming Growth Factor alpha

Identifiers

PMID22667988
PMCPMC3789377
OpenAlexW2030696041

What OpenQuestion holds

Textmetadata
LicenceTDM
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.