Evidence map›Paper›PMID 31195016›Full record

ReviewJournal of molecular biology2020

Ribosome Abundance Control Via the Ubiquitin-Proteasome System and Autophagy.

Heeseon An, J Wade Harper

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
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  9. Review
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  11. Review
  12. Review
  13. Article
  14. Article
  15. Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  16. Rpl12 is a conserved ribophagy receptor.Nature cell biology · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. How total mRNA influences cell growth.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

2 authors at 1 institution in 1 country.

Heeseon AnDepartment of Cell Biology, Blavatnik Institute at Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA.
J Wade HarperDepartment of Cell Biology, Blavatnik Institute at Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA. Electronic address: wade_harper@hms.harvard.edu.
Harvard University · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
Network organization of the human autophagy systemR01GM095567 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W, KIMMELMAN, ALEC · 2011 to 2018
$3.0M
Systematic discovery and functional analysis of the PARKIN modified proteomeR37NS083524 · NINDS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W · 2013 to 2019
$3.0M
NCI NIH HHS P30 CA016087NIA NIH HHS R01 AG011085NIGMS NIH HHS R01 GM095567NINDS NIH HHS R37 NS083524
6 · The paper itself

Abstract

Ribosomes are central to the life of a cell, as they translate the genetic code into the amino acid language of proteins. Moreover, ribosomal abundance within the cell is coordinated with protein production required for cell function or processes such as cell division. As such, it is not surprising that these elegant machines are both highly regulated at the level of both their output of newly translated proteins but also at the level of ribosomal protein expression, ribosome assembly, and ribosome turnover. In this review, we focus on mechanisms that regulate ribosome abundance through both the ubiquitin-proteasome system and forms of autophagy referred to as "ribophagy." We discussed mechanisms employed in both yeast and mammalian cells, including the various machineries that are important for recognition and degradation of ribosomal components. In addition, we discussed controversies in the field and how the development of new approaches for examining flux through the proteasomal and autophagic systems in the context of a systematic inventory of ribosomal components is necessary to fully understand how ribosome abundance is controlled under various physiological conditions.

Indexed as

AnimalsAutophagyCell DivisionMammalsProteasome Endopeptidase ComplexProteolysisRibosomal ProteinsRibosomesSaccharomyces cerevisiaeUbiquitinProteasome Endopeptidase ComplexRibosomal ProteinsUbiquitinautophagydegradationribosomeubiquitin

Identifiers

PMID31195016
PMCPMC6904543
OpenAlexW2949232106

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.