Evidence map›Paper›PMID 21079247›Full record

ArticleThe Journal of cell biology2010

Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering.

Margarita Cabrera, Lars Langemeyer, Muriel Mari, Ralf Rethmeier, Ioan Orban, Angela Perz, Cornelia Bröcker, Janice Griffith, Daniel Klose, Heinz-Jürgen Steinhoff and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.9field-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

72 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Regulation of vacuole fusion in stomata by dephosphorylation of the HOPS subunit VPS39.The Plant journal : for cell and molecular biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. TbVps41 regulates trafficking of endocytic but not biosynthetic cargo to lysosomes of bloodstream forms of Trypanosoma brucei.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article

12 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

13 authors at 2 institutions in 2 countries.

Margarita CabreraDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, 49076 Osnabrück, Germany.
Lars Langemeyer
Muriel Mari
Ralf Rethmeier
Ioan Orban
Angela Perz
Cornelia Bröcker
Janice Griffith
Daniel Klose
Heinz-Jürgen Steinhoff
Fulvio Reggiori
Siegfried Engelbrecht-Vandré
Christian Ungermann
Osnabrück University · DEUniversity Medical Center Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tethering factors are organelle-specific multisubunit protein complexes that identify, along with Rab guanosine triphosphatases, transport vesicles and trigger their SNARE-mediated fusion of specific transport vesicles with the target membranes. Little is known about how tethering factors discriminate between different trafficking pathways, which may converge at the same organelle. In this paper, we describe a phosphorylation-based switch mechanism, which allows the homotypic vacuole fusion protein sorting effector subunit Vps41 to operate in two distinct fusion events, namely endosome-vacuole and AP-3 vesicle-vacuole fusion. Vps41 contains an amphipathic lipid-packing sensor (ALPS) motif, which recognizes highly curved membranes. At endosomes, this motif is inserted into the lipid bilayer and masks the binding motif for the δ subunit of the AP-3 complex, Apl5, without affecting the Vps41 function in endosome-vacuole fusion. At the much less curved vacuole, the ALPS motif becomes available for phosphorylation by the resident casein kinase Yck3. As a result, the Apl5-binding site is exposed and allows AP-3 vesicles to bind to Vps41, followed by specific fusion with the vacuolar membrane. This multifunctional tethering factor thus discriminates between trafficking routes by switching from a curvature-sensing to a coat recognition mode upon phosphorylation.

Indexed as

Amino Acid MotifsAnimalsCasein Kinase ICell MembraneEndosomesMolecular Sequence DataMultiprotein ComplexesPhosphorylationrab GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentVacuolesVesicular Transport ProteinsCasein Kinase IMultiprotein Complexesrab GTP-Binding ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS41 protein, S cerevisiaeYCK3 protein, S cerevisiae

Identifiers

PMID21079247
PMCPMC2983053
OpenAlexW2121560523

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.