Evidence map›Paper›PMID 27839950›Full record

ArticleStructure (London, England : 1993)2016

Structural Basis for Selective Interaction between the ESCRT Regulator HD-PTP and UBAP1.

Deepankar Gahloth, Colin Levy, Graham Heaven, Flavia Stefani, Lydia Wunderley, Paul Mould, Matthew J Cliff, Jordi Bella, Alistair J Fielding, Philip Woodman and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-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

20 citing papers in PubMed, 25 citations in OpenAlex.

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  20. AThe EMBO journal · 2017
    Article
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

11 authors at 1 institution in 1 country.

Deepankar GahlothSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Colin LevySchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Graham HeavenSchool of Chemistry and Photon Science Institute, University of Manchester, Manchester M13 9PT, UK.
Flavia StefaniSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Lydia WunderleySchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Paul MouldSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Matthew J CliffSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Jordi BellaSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester M13 9PT, UK.
Alistair J FieldingSchool of Chemistry and Photon Science Institute, University of Manchester, Manchester M13 9PT, UK.
Philip WoodmanSchool of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, 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 M13 9PT, UK. Electronic address: lydia.tabernero@manchester.ac.uk.
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E019919/1Medical Research Council G0701140Medical Research Council MR/K011049/1
6 · The paper itself

Abstract

Endosomal sorting complexes required for transport (ESCRTs) are essential for ubiquitin-dependent degradation of mitogenic receptors, a process often compromised in cancer pathologies. Sorting of ubiquinated receptors via ESCRTs is controlled by the tumor suppressor phosphatase HD-PTP. The specific interaction between HD-PTP and the ESCRT-I subunit UBAP1 is critical for degradation of growth factor receptors and integrins. Here, we present the structural characterization by X-ray crystallography and double electron-electron resonance spectroscopy of the coiled-coil domain of HD-PTP and its complex with UBAP1. The coiled-coil domain adopts an unexpected open and rigid conformation that contrasts with the closed and flexible coiled-coil domain of the related ESCRT regulator Alix. The HD-PTP:UBAP1 structure identifies the molecular determinants of the interaction and provides a molecular basis for the specific functional cooperation between HD-PTP and UBAP1. Our findings provide insights into the molecular mechanisms of regulation of ESCRT pathways that could be relevant to anticancer therapies.

Indexed as

Binding SitesCarrier ProteinsCrystallography, X-RayEndosomal Sorting Complexes Required for TransportHumansModels, MolecularProtein BindingProtein Structure, SecondaryProtein Tyrosine Phosphatases, Non-ReceptorCarrier ProteinsEndosomal Sorting Complexes Required for TransportProtein Tyrosine Phosphatases, Non-ReceptorPTPN23 protein, humanUBAP1 protein, humancoiled-coil structureendosomal ESCRTs regulationmitogenic signaling downregulationtumor suppressor phosphataseubiquitin-dependent trafficking

Identifiers

PMID27839950
PMCPMC5145805
OpenAlexW2551500169

What Socratic 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 Socratic graph.