Evidence map›Paper›PMID 28564595›Full record

ArticleCell reports2017

Structural Basis for Regulation of ESCRT-III Complexes by Lgd.

Brian J McMillan, Christine Tibbe, Andrew A Drabek, Tom C M Seegar, Stephen C Blacklow, Thomas Klein

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  3. Article
  4. Notch Signaling in Drosophila Tumor Models.Advances in experimental medicine and biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. UsingInternational journal of molecular sciences · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Monoallelic Mutations inCirculation. Genomic and precision medicine · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. ESCRT-dependent control of membrane remodelling during cell division.Seminars in cell & developmental biology · 2018
    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

6 authors at 3 institutions in 2 countries.

Brian J McMillanDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Christine TibbeInstitute of Genetics, Heinrich-Heine-University, Dusseldorf 40225, Germany.
Andrew A DrabekDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Tom C M SeegarDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Stephen C BlacklowDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA; Dana Farber Cancer Institute, Department of Cancer Biology, Boston, MA 02215, USA. Electronic address: stephen_blacklow@hms.harvard.edu.
Thomas KleinInstitute of Genetics, Heinrich-Heine-University, Dusseldorf 40225, Germany. Electronic address: thomas.klein@uni-duesseldorf.de.
Harvard University · USHeinrich Heine University Düsseldorf · DEDana-Farber Cancer Institute · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Protein CoreP01CA119070 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI ASTER, JON C. · 2006 to 2016
$10.3M
Structure and Function in Notch SignalingR01CA092433 · NCI · HARVARD MEDICAL SCHOOL · PI BLACKLOW, STEPHEN C. · 2002 to 2016
$5.0M
NCI NIH HHS P01 CA119070NCI NIH HHS R01 CA092433NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

The ESCRT-III complex induces outward membrane budding and fission through homotypic polymerization of its core component Shrub/CHMP4B. Shrub activity is regulated by its direct interaction with a protein called Lgd in flies, or CC2D1A or B in humans. Here, we report the structural basis for this interaction and propose a mechanism for regulation of polymer assembly. The isolated third DM14 repeat of Lgd binds Shrub, and an Lgd fragment containing only this DM14 repeat and its C-terminal C2 domain is sufficient for in vivo function. The DM14 domain forms a helical hairpin with a conserved, positively charged tip, that, in the structure of a DM14 domain-Shrub complex, occupies a negatively charged surface of Shrub that is otherwise used for homopolymerization. Lgd mutations at this interface disrupt its function in flies, confirming functional importance. Together, these data argue that Lgd regulates ESCRT activity by controlling access to the Shrub self-assembly surface.

Indexed as

AnimalsCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsEndosomal Sorting Complexes Required for TransportModels, MolecularMutationNerve Tissue ProteinsProtein BindingProtein DomainsStructure-Activity RelationshipTumor Suppressor ProteinsDrosophila ProteinsEndosomal Sorting Complexes Required for Transportl(2)gd1 protein, DrosophilaNerve Tissue ProteinsShrb protein, DrosophilaTumor Suppressor ProteinsCC2D1ACC2D1BCHMP4BDM14 domainlethal giant discsmembrane fissionmultivesicular bodyShrubSnf7

Identifiers

PMID28564595
PMCPMC5528166
OpenAlexW2619644271

What OpenQuestion holds

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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.