Evidence map›Paper›PMID 30955882›Full record

ArticleCell2019

ATG8-Binding UIM Proteins Define a New Class of Autophagy Adaptors and Receptors.

Richard S Marshall, Zhihua Hua, Sujina Mali, Fionn McLoughlin, Richard D Vierstra

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 172 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
172citing papers in PubMed, 1 pooled it
28.7field-weighted citation impact, top 1% 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

172 citing papers in PubMed, 1 synthesis or guideline pooled it, 295 citations in OpenAlex.

  1. Guideline
  2. Plant direct · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Biomolecular condensation of ERC1 recruits ATG8 and NBR1 to drive autophagosome formation for plant heat tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Targeted Degradation Technologies Utilizing Autophagy.International journal of molecular sciences · 2025
    Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Mechanisms and roles of membrane-anchored ATG8s.Frontiers in cell and developmental biology · 2025
    Review
  20. Article

112 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Richard S MarshallDepartment of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA.
Zhihua HuaDepartment of Environmental and Plant Biology, Ohio University, Athens, OH 45701, USA.
Sujina MaliDepartment of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA.
Fionn McLoughlinDepartment of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA.
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA. Electronic address: rdvierstra@wustl.edu.
Washington University in St. Louis · USOhio University · US

Funding

Autophagic Clearance of Proteasomes and CDC48 as Models for Amyloidogenic Protein Quality Control.R01GM124452 · NIGMS · WASHINGTON UNIVERSITY · PI JEZ, JOSEPH MARTIN · 2018 to 2025
$2.4M
NIGMS NIH HHS R01 GM124452
6 · The paper itself

Abstract

During autophagy, vesicle dynamics and cargo recruitment are driven by numerous adaptors and receptors that become tethered to the phagophore through interactions with lipidated ATG8/LC3 decorating the expanding membrane. Most currently described ATG8-binding proteins exploit a well-defined ATG8-interacting motif (AIM, or LC3-interacting region [LIR]) that contacts a hydrophobic patch on ATG8 known as the LIR/AIM docking site (LDS). Here we describe a new class of ATG8 interactors that exploit ubiquitin-interacting motif (UIM)-like sequences for high-affinity binding to an alternative ATG8 interaction site. Assays with candidate UIM-containing proteins together with unbiased screens identified a large collection of UIM-based ATG8 interactors in plants, yeast, and humans. Analysis of a subset also harboring ubiquitin regulatory X (UBX) domains revealed a role for UIM-directed autophagy in clearing non-functional CDC48/p97 complexes, including some impaired in human disease. With this new class of adaptors and receptors, we greatly extend the reach of selective autophagy and identify new factors regulating autophagic vesicle dynamics.

Indexed as

AutophagyAmino Acid MotifsArabidopsisArabidopsis ProteinsAutophagy-Related Protein 8 FamilyBinding SitesHumansMicrotubule-Associated ProteinsProtein BindingProtein Interaction Domains and MotifsProtein Structure, TertiaryRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentArabidopsis ProteinsAutophagy-Related Protein 8 FamilyMicrotubule-Associated ProteinsPSMD4 protein, humanRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsAIMArabidopsisATG8ATG8-interacting motifautophagyCDC48/p97LC3-interacting regionLDSLIRLIR/AIM-docking siteubiquitin-interacting motifUDSUIMUIM-docking siteyeast

Identifiers

PMID30955882
PMCPMC6810650
OpenAlexW2935272799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.