Evidence map›Paper›PMID 22918958›Full record

ArticleMolecular biology of the cell2012

Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes.

Joëlle Morvan, Bruno Rinaldi, Sylvie Friant

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Review
  2. Review
  3. The Machinery of Exosomes: Biogenesis, Release, and Uptake.International journal of molecular sciences · 2023
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Exosomes genetic cargo in lung cancer: a truly Pandora's box.Translational lung cancer research · 2016
    Review
  17. Review
  18. Vps1 in the late endosome-to-vacuole traffic.Journal of biosciences · 2013
    Article
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

3 authors.

Joëlle MorvanDepartment of Molecular and Cellular Genetics, Unité Mixte de Recherche 7156, Université de Strasbourg and Centre National de la Recherche Scientifique, 67084 Strasbourg, France. morvan@igbmc.fr
Bruno Rinaldi
Sylvie Friant

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multivesicular endosomes (MVBs) are major sorting platforms for membrane proteins and participate in plasma membrane protein turnover, vacuolar/lysosomal hydrolase delivery, and surface receptor signal attenuation. MVBs undergo unconventional inward budding, which results in the formation of intraluminal vesicles (ILVs). MVB cargo sorting and ILV formation are achieved by the concerted function of endosomal sorting complex required for transport (ESCRT)-0 to ESCRT-III. The ESCRT-0 subunit Vps27 is a key player in this pathway since it recruits the other complexes to endosomes. Here we show that the Pkh1/Phk2 kinases, two yeast orthologues of the 3-phosphoinositide-dependent kinase, phosphorylate directly Vps27 in vivo and in vitro. We identify the phosphorylation site as the serine 613 and demonstrate that this phosphorylation is required for proper Vps27 function. Indeed, in pkh-ts temperature-sensitive mutant cells and in cells expressing vps27(S613A), MVB sorting of the carboxypeptidase Cps1 and of the α-factor receptor Ste2 is affected and the Vps28-green fluorescent protein ESCRT-I subunit is mainly cytoplasmic. We propose that Vps27 phosphorylation by Pkh1/2 kinases regulates the coordinated cascade of ESCRT complex recruitment at the endosomal membrane.

Indexed as

3-Phosphoinositide-Dependent Protein KinasesEndosomal Sorting Complexes Required for TransportEndosomesGreen Fluorescent ProteinsMultivesicular BodiesMutationPhosphorylationPhosphoserineProtein Serine-Threonine KinasesProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins3-Phosphoinositide-Dependent Protein KinasesEndosomal Sorting Complexes Required for TransportGreen Fluorescent ProteinsPhosphoserinePKH1 protein, S cerevisiaePKH2 protein, S cerevisiaeProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsVPS27 protein, S cerevisiae

Identifiers

PMID22918958
PMCPMC3469520

What OpenQuestion holds

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Registered trials

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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.