Evidence map›Paper›PMID 17429078›Full record

ArticleMolecular biology of the cell2007

Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase rsp5 to membrane proteins in vivo and in vitro.

James A Sullivan, Michael J Lewis, Elina Nikko, Hugh R B Pelham

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  3. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Sodium Acetate Responses inFrontiers in microbiology · 2018
    Review
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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

4 authors at 1 institution in 1 country.

James A SullivanMedical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Michael J Lewis
Elina Nikko
Hugh R B Pelham
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178788
6 · The paper itself

Abstract

Recognition of membrane proteins by the Nedd4/Rsp5 ubiquitin ligase family is a critical step in their targeting to the multivesicular body pathway. Some substrates contain "PY" motifs (PPxY), which bind to WW domains in the ligase. Others lack PY motifs and instead rely on adaptors that recruit the ligase to them. To investigate the mechanism of adaptor-mediated ubiquitination, we have characterized the interactions between the adaptor Bsd2, the ubiquitin ligase Rsp5, and the membrane proteins Cps1, Tre1, and Smf1 from Saccharomyces cerevisiae. We have reconstituted adaptor-mediated modification of Cps1 and Tre1 in vitro, and we show that two PY motifs in Bsd2 and two WW domains (WW2 and WW3) in Rsp5 are crucial for this. The binding of a weak noncanonical DMAPSY motif in Bsd2 to WW3 is an absolute requirement for Bsd2 adaptor function. We show that sorting of the manganese transporter Smf1, which requires both Bsd2 and Tre1, depends upon two PY motifs in Bsd2 and one motif in Tre1 but only two WW domains in Rsp5. We suggest that sequential assembly of first a Bsd2/Rsp5 complex, then a Tre1/Bsd2/Rsp5 complex followed by a rearrangement of PY-WW interactions is required for the ubiquitination of Smf1.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceEndosomal Sorting Complexes Required for TransportMembrane ProteinsModels, BiologicalMutationProtein BindingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesAdaptor Proteins, Signal TransducingEndosomal Sorting Complexes Required for TransportMembrane ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase Complexes

Identifiers

PMID17429078
PMCPMC1924809
OpenAlexW2124438628

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.