Evidence map›Paper›PMID 28602823›Full record

ArticleStructure (London, England : 1993)2017

Structural Basis for Specific Interaction of TGFβ Signaling Regulators SARA/Endofin with HD-PTP.

Deepankar Gahloth, Colin Levy, Louise Walker, Lydia Wunderley, A Paul Mould, Sandra Taylor, Philip Woodman, Lydia Tabernero

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Deepankar GahlothSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
Colin LevySchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
Louise WalkerSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
Lydia WunderleySchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
A Paul MouldSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
Sandra TaylorSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK.
Philip WoodmanSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK. Electronic address: philip.woodman@manchester.ac.uk.
Lydia TaberneroSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester M13 9PT, UK. Electronic address: lydia.tabernero@manchester.ac.uk.
Manchester Academic Health Science Centre · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K008773/1Medical Research Council G0701140Medical Research Council MR/K011049/1
6 · The paper itself

Abstract

SARA and endofin are endosomal adaptor proteins that drive Smad phosphorylation by ligand-activated transforming growth factor β/bone morphogenetic protein (TGFβ/BMP) receptors. We show in this study that SARA and endofin also recruit the tumor supressor HD-PTP, a master regulator of endosomal sorting and ESCRT-dependent receptor downregulation. High-affinity interactions occur between the SARA/endofin N termini, and the conserved hydrophobic region in the HD-PTP Bro1 domain that binds CHMP4/ESCRT-III. CHMP4 engagement is a universal feature of Bro1 proteins, but SARA/endofin binding is specific to HD-PTP. Crystallographic structures of HD-PTP

Indexed as

Molecular Docking SimulationBinding SitesEndosomal Sorting Complexes Required for TransportHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsProtein BindingProtein Tyrosine Phosphatases, Non-ReceptorSerine EndopeptidasesTransforming Growth Factor betaCHMP4B protein, humanEndosomal Sorting Complexes Required for TransportIntracellular Signaling Peptides and ProteinsProtein Tyrosine Phosphatases, Non-ReceptorPTPN23 protein, humanSerine EndopeptidasesTransforming Growth Factor betaZFYVE16 protein, humancrystallographic structuresendosomal effectorsESCRT-IIISARA and endofinTGFβ signalingtumor-supressor phosphatase

Identifiers

PMID28602823
PMCPMC5501724
OpenAlexW2624001846

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.