Evidence map›Paper›PMID 33351099›Full record

ArticleThe Journal of cell biology2021

A selective transmembrane recognition mechanism by a membrane-anchored ubiquitin ligase adaptor.

Felichi Mae Arines, Aaron Jeremy Hamlin, Xi Yang, Yun-Yu Jennifer Liu, Ming Li

Abstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Lysosomal Repair in Health and Disease.Journal of cellular physiology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. The Ubiquitin Switch in Plant Stress Response.Plants (Basel, Switzerland) · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Felichi Mae ArinesDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.
Aaron Jeremy HamlinDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.
Xi YangDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.
Yun-Yu Jennifer LiuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.
Ming LiDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI.

Funding

Undergrad supplement: Ubiquitin-Dependent Protein Regulation and Quality Control of the Lysosomal MembraneR01GM133873 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LI, MING · 2019 to 2023
$1.9M
NIGMS NIH HHS R01 GM133873
6 · The paper itself

Abstract

While it is well-known that E3 ubiquitin ligases can selectively ubiquitinate membrane proteins in response to specific environmental cues, the underlying mechanisms for the selectivity are poorly understood. In particular, the role of transmembrane regions, if any, in target recognition remains an open question. Here, we describe how Ssh4, a yeast E3 ligase adaptor, recognizes the PQ-loop lysine transporter Ypq1 only after lysine starvation. We show evidence of an interaction between two transmembrane helices of Ypq1 (TM5 and TM7) and the single transmembrane helix of Ssh4. This interaction is regulated by the conserved PQ motif. Strikingly, recent structural studies of the PQ-loop family have suggested that TM5 and TM7 undergo major conformational changes during substrate transport, implying that transport-associated conformational changes may determine the selectivity. These findings thus provide critical information concerning the regulatory mechanism through which transmembrane domains can be specifically recognized in response to changing environmental conditions.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceBinding SitesCell MembraneGenes, SuppressorGreen Fluorescent ProteinsModels, BiologicalMutagenesisMutationProtein Structure, SecondaryProteolysisReproducibility of ResultsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, ProteinUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingGreen Fluorescent ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID33351099
PMCPMC7759299

What OpenQuestion holds

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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.