Evidence map›Paper›PMID 35364016›Full record

ReviewMolecular cell2022

Mechanisms underlying ubiquitin-driven selective mitochondrial and bacterial autophagy.

Ellen A Goodall, Felix Kraus, J Wade Harper

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
14.5field-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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. SMURF2 inhibits autophagic control ofbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Endogenous LRRK2 and PINK1 function in a convergent neuroprotective ciliogenesis pathway in the brain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Ubiquitin and Ubiquitin-Like Modifications in Organelle Stress Signaling: Ub, Ub, Ub, Ub, Stayin' Alive, Stayin' Alive.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  19. Deletion of the E3 ubiquitin ligase LRSAM1 fosters intracellularFrontiers in cellular and infection microbiology · 2025
    Article
  20. 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 at 1 institution in 1 country.

Ellen A GoodallDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Felix KrausDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Aligning Science Across Parkinson's (ASAP) Collaborative Research Network, Chevy Chase, MD 20815, USA.
J Wade HarperDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Aligning Science Across Parkinson's (ASAP) Collaborative Research Network, Chevy Chase, MD 20815, USA. Electronic address: wade_harper@hms.harvard.edu.
Harvard University · US

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
Systematic Exploration of the Human Interactome IVU24HG006673 · NHGRI · HARVARD MEDICAL SCHOOL · PI GYGI, STEVEN P, HARPER, JEFFREY W · 2018 to 2025
$6.0M
Endolysosomal Proteome Landscapes Through the Lens of Neurodegenerative Risk AllelesR01NS110395 · NINDS · HARVARD MEDICAL SCHOOL · PI JEFFREY W HARPER · 2018 to 2026
$4.1M
Systematic discovery and functional analysis of the PARKIN modified proteomeR37NS083524 · NINDS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W · 2013 to 2019
$3.0M
Regulation of PINK1 and PARKIN-Dependent MitophagyR01NS083524 · NINDS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W · 2020 to 2024
$2.2M
NHGRI NIH HHS U24 HG006673NIA NIH HHS R01 AG011085NINDS NIH HHS R01 NS083524NINDS NIH HHS R01 NS110395NINDS NIH HHS R37 NS083524
6 · The paper itself

Abstract

Selective autophagy specifically eliminates damaged or superfluous organelles, maintaining cellular health. In this process, a double membrane structure termed an autophagosome captures target organelles or proteins and delivers this cargo to the lysosome for degradation. The attachment of the small protein ubiquitin to cargo has emerged as a common mechanism for initiating organelle or protein capture by the autophagy machinery. In this process, a suite of ubiquitin-binding cargo receptors function to initiate autophagosome assembly in situ on the target cargo, thereby providing selectivity in cargo capture. Here, we review recent efforts to understand the biochemical mechanisms and principles by which cargo are marked with ubiquitin and how ubiquitin-binding cargo receptors use conserved structural modules to recruit the autophagosome initiation machinery, with a particular focus on mitochondria and intracellular bacteria as cargo. These emerging mechanisms provide answers to long-standing questions in the field concerning how selectivity in cargo degradation is achieved.

Indexed as

MitophagyUbiquitinAutophagyBacteriaMitochondriaUbiquitincargo receptormitophagyselective autophagyubiquitinxenophagy

Identifiers

PMID35364016
PMCPMC9254164
OpenAlexW4220684596

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.