Evidence map›Paper›PMID 27852901›Full record

ArticleMolecular biology of the cell2017

Multivalent Rab interactions determine tether-mediated membrane fusion.

Anna Lürick, Jieqiong Gao, Anne Kuhlee, Erdal Yavavli, Lars Langemeyer, Angela Perz, Stefan Raunser, Christian Ungermann

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.1field-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

40 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  3. SNX-3 confers lysosomal fusion-competence to sustain basal autophagy.Cellular and molecular life sciences : CMLS · 2026
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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.

Anna LürickBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Jieqiong GaoBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Anne KuhleeDepartment of Physical Biochemistry, Max-Planck Institute of Molecular Physiology; 44227 Dortmund, Germany.
Erdal YavavliBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Lars LangemeyerBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Angela PerzBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Stefan RaunserDepartment of Physical Biochemistry, Max-Planck Institute of Molecular Physiology; 44227 Dortmund, Germany.
Christian UngermannBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany cu@uos.de.
Osnabrück University · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane fusion at endomembranes requires cross-talk between Rab GTPases and tethers to drive SNARE-mediated lipid bilayer mixing. Several tethers have multiple Rab-binding sites with largely untested function. Here we dissected the lysosomal HOPS complex as a tethering complex with just two binding sites for the Rab7-like Ypt7 protein to determine their relevance for fusion. Using tethering and fusion assays combined with HOPS mutants, we show that HOPS-dependent fusion requires both Rab-binding sites, with Vps39 being the stronger Ypt7 interactor than Vps41. The intrinsic amphipathic lipid packaging sensor (ALPS) motif within HOPS Vps41, a target of the vacuolar kinase Yck3, is dispensable for tethering and fusion but can affect tethering if phosphorylated. In combination, our data demonstrate that a multivalent tethering complex uses its two Rab bindings to determine the place of SNARE assembly and thus fusion at endomembranes.

Indexed as

Binding SitesEndosomesMembrane FusionPhosphorylationProtein BindingProtein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVacuolesVesicular Transport Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVesicular Transport ProteinsYPT7 protein, S cerevisiae

Identifiers

PMID27852901
PMCPMC5231900
OpenAlexW2550692097

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.