Evidence map›Paper›PMID 23901104›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural basis of Vps33A recruitment to the human HOPS complex by Vps16.

Stephen C Graham, Lena Wartosch, Sally R Gray, Edward J Scourfield, Janet E Deane, J Paul Luzio, David J Owen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 101 citations in OpenAlex.

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  18. Modeling of Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  19. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
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  20. Article

2 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Stephen C GrahamDepartment of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, United Kingdom. scg34@cam.ac.uk
Lena Wartosch
Sally R Gray
Edward J Scourfield
Janet E Deane
J Paul Luzio
David J Owen
University of Cambridge · GB

Funding

Medical Research Council G0900113Wellcome Trust 090909Wellcome Trust 090909/Z/09/ZWellcome Trust 098406/Z/12/ZWellcome Trust 100140
6 · The paper itself

Abstract

The multisubunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is required for late endosome-lysosome and autophagosome-lysosome fusion in mammals. We have determined the crystal structure of the human HOPS subunit Vps33A, confirming its identity as a Sec1/Munc18 family member. We show that HOPS subunit Vps16 recruits Vps33A to the human HOPS complex and that residues 642-736 are necessary and sufficient for this interaction, and we present the crystal structure of Vps33A in complex with Vps16(642-736). Mutations at the binding interface disrupt the Vps33A-Vps16 interaction both in vitro and in cells, preventing recruitment of Vps33A to the HOPS complex. The Vps33A-Vps16 complex provides a structural framework for studying the association between Sec1/Munc18 proteins and tethering complexes.

Indexed as

Models, MolecularProtein ConformationBinding SitesEscherichia coliHumansMultiprotein ComplexesMutationSpecies SpecificityVesicular Transport ProteinsMultiprotein ComplexesVesicular Transport ProteinsVPS16 protein, humanVPS33A protein, human

Identifiers

PMID23901104
PMCPMC3746937
OpenAlexW2142846853

What OpenQuestion holds

Textmetadata
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.