Evidence map›Paper›PMID 17645729›Full record

ArticleTraffic (Copenhagen, Denmark)2007

Targeting of Sna3p to the endosomal pathway depends on its interaction with Rsp5p and multivesicular body sorting on its ubiquitylation.

Marta Stawiecka-Mirota, Wojciech Pokrzywa, Joelle Morvan, Teresa Zoladek, Rosine Haguenauer-Tsapis, Danièle Urban-Grimal, Pierre Morsomme

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Membrane trafficking in the yeast Saccharomyces cerevisiae model.International journal of molecular sciences · 2015
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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

7 authors.

Marta Stawiecka-MirotaInstitut Jacques Monod, CNRS, Universités Paris VI et VII, Département de Biologie Cellulaire, 2 Place Jussieu 75005 Paris, France.
Wojciech Pokrzywa
Joelle Morvan
Teresa Zoladek
Rosine Haguenauer-Tsapis
Danièle Urban-Grimal
Pierre Morsomme

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rsp5p is an ubiquitin (Ub)-protein ligase of the Nedd4 family that carries WW domains involved in interaction with PPXY-containing proteins. It plays a key role at several stages of intracellular trafficking, such as Ub-mediated internalization of endocytic cargoes and Ub-mediated sorting of membrane proteins to internal vesicles of multivesicular bodies (MVBs), a process that is crucial for their subsequent targeting to the vacuolar lumen. Sna3p is a membrane protein previously described as an Ub-independent MVB cargo, but proteomic studies have since shown it to be an ubiquitylated protein. Sna3p carries a PPXY motif. We observed that this motif mediates its interaction with Rsp5p WW domains. Mutation of either the Sna3p PPXY motif or the Rsp5p WW3 domain or reduction in the amounts of Rsp5 results in the mistargeting of Sna3p to multiple mobile vesicles and prevents its sorting to the endosomal pathway. This sorting defect appears to occur prior to the defect displayed in rsp5 mutants by other MVB cargoes, which are correctly sorted to the endosomal pathway but missorted to the vacuolar membrane instead of the vacuolar lumen. Sna3p is polyubiquitylated on one target lysine, and a mutant Sna3p lacking its target lysine displays defective MVB sorting. Sna3p undergoes Rsp5-dependent polyubiquitylation, with K63-linked Ub chains.

Indexed as

Binding SitesEndosomal Sorting Complexes Required for TransportEndosomesImmunoprecipitationLysineMembrane ProteinsMutationProtein BindingProtein Processing, Post-TranslationalProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransport VesiclesUbiquitinUbiquitin-Protein Ligase ComplexesEndosomal Sorting Complexes Required for TransportLysineMembrane ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSna3 protein, S cerevisiaeUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

PMID17645729
PMCPMC2171029

What OpenQuestion holds

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Read underepoch 390

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.