Evidence map›Paper›PMID 9606181›Full record

ArticleThe EMBO journal1998

The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function.

M Babst, B Wendland, E J Estepa, S D Emr

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 424 papers.

0numbers the graph read from it
0cells of the map it votes in
424citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

424 citing papers in PubMed, 756 citations in OpenAlex.

  1. Article
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  7. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
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  18. Cryo-EM structure of AAA + ATPase thorase reveals novel helical filament formation.Computational and structural biotechnology journal · 2025
    Article
  19. Relationship between exosomes and cancer: formation, diagnosis, and treatment.International journal of biological sciences · 2025
    Review
  20. Article

364 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

4 authors at 1 institution in 1 country.

M BabstDivision of Cellular Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego, School of Medicine La Jolla, CA 92093-0668, USA.
B Wendland
E J Estepa
S D Emr
University of California, San Diego · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
NCI NIH HHS CA58689
6 · The paper itself

Abstract

Vps4p is an AAA-type ATPase required for efficient transport of biosynthetic and endocytic cargo from an endosome to the lysosome-like vacuole of Saccharomyces cerevisiae. Vps4p mutants that do not bind ATP or are defective in ATP hydrolysis were characterized both in vivo and in vitro. The nucleotide-free or ADP-bound form of Vps4p existed as a dimer, whereas in the ATP-locked state, Vps4p dimers assembled into a decameric complex. This suggests that ATP hydrolysis drives a cycle of association and dissociation of Vps4p dimers/decamers. Nucleotide binding also regulated the association of Vps4p with an endosomal compartment in vivo. This membrane association required the N-terminal coiled-coil motif of Vps4p, but deletion of the coiled-coil domain did not affect ATPase activity or oligomeric assembly of the protein. Membrane association of two previously uncharacterized class E Vps proteins, Vps24p and Vps32p/Snf7p, was also affected by mutations in VPS4. Upon inactivation of a temperature-conditional vps4 mutant, Vps24p and Vps32p/Snf7p rapidly accumulated in a large membrane-bound complex. Immunofluorescence indicated that both proteins function with Vps4p at a common endosomal compartment. Together, the data suggest that the Vps4 ATPase catalyzes the release (uncoating) of an endosomal membrane-associated class E protein complex(es) required for normal morphology and sorting activity of the endosome.

Indexed as

Nuclear ProteinsSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateDimerizationEndosomal Sorting Complexes Required for TransportEndosomesEnzyme ActivationFungal ProteinsIntracellular MembranesMacromolecular SubstancesNucleotidesPolymersProtein BindingSaccharomyces cerevisiaeSubcellular FractionsAdenosine TriphosphatasesAdenosine TriphosphateEndosomal Sorting Complexes Required for TransportFungal ProteinsMacromolecular SubstancesNuclear ProteinsNucleotidesPolymersSaccharomyces cerevisiae ProteinsSNF7 protein, S cerevisiaeVPS4 protein, S cerevisiae

Identifiers

PMID9606181
PMCPMC1170638
OpenAlexW2003979167

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.