Evidence map›Paper›PMID 28831121›Full record

ArticleScientific reports2017

The open architecture of HD-PTP phosphatase provides new insights into the mechanism of regulation of ESCRT function.

Deepankar Gahloth, Graham Heaven, Thomas A Jowitt, A Paul Mould, Jordi Bella, Clair Baldock, Philip Woodman, Lydia Tabernero

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Pseudophosphatases as Regulators of MAPK Signaling.International journal of molecular sciences · 2021
    Review
  11. Article
  12. The Roles of Pseudophosphatases in Disease.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Shedding Light on Extracellular Vesicle Biogenesis and Bioengineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Review
  17. The many functions of ESCRTs.Nature reviews. Molecular cell biology · 2020
    Review
  18. Article
  19. Article
  20. Review
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, UK.
Graham HeavenSchool of Chemistry and Photon Science Institute, University of Manchester, Manchester, UK.
Thomas A JowittSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
A Paul MouldSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
Jordi BellaSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
Clair BaldockSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
Philip WoodmanSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
Lydia TaberneroSchool of Biological Sciences, Faculty of Biology Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK. lydia.tabernero@manchester.ac.uk.
University of Manchester · GBManchester Academic Health Science Centre · GB

Funding

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

Abstract

HD-PTP is a tumour suppressor phosphatase that controls endocytosis, down-regulation of mitogenic receptors and cell migration. Central to its role is the specific recruitment of critical endosomal sorting complexes required for transport (ESCRTs). However, the molecular mechanisms that enable HD-PTP to regulate ESCRT function are unknown. We have characterised the molecular architecture of the entire ESCRT binding region of HD-PTP using small angle X-ray scattering and hydrodynamic analyses. We show that HD-PTP adopts an open and extended conformation, optimal for concomitant interactions with multiple ESCRTs, which contrasts with the compact conformation of the related ESCRT regulator Alix. We demonstrate that the HD-PTP open conformation is functionally competent for binding cellular protein partners. Our analyses rationalise the functional cooperation of HD-PTP with ESCRT-0, ESCRT-I and ESCRT-III and support a model for regulation of ESCRT function by displacement of ESCRT subunits, which is crucial in determining the fate of ubiquitinated cargo.

Indexed as

Endosomal Sorting Complexes Required for TransportHydrodynamicsModels, MolecularProtein BindingProtein ConformationProtein Tyrosine Phosphatases, Non-ReceptorScattering, Small AngleX-Ray DiffractionEndosomal Sorting Complexes Required for TransportProtein Tyrosine Phosphatases, Non-Receptor

Identifiers

PMID28831121
PMCPMC5567221
OpenAlexW2748147636

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.