Evidence map›Paper›PMID 32881044›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2020

Ubiquitin-Modulated Phase Separation of Shuttle Proteins: Does Condensate Formation Promote Protein Degradation?

Thuy P Dao, Carlos A Castañeda

Open access · greenAbstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Phase separation of polyubiquitinated proteins in UBQLN2 condensates controls substrate fate.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Article
  14. Article
  15. TheActa biochimica et biophysica Sinica · 2023
    Article
  16. Article
  17. Decoding optimal ligand design for multicomponent condensates.bioRxiv : the preprint server for biology · 2023
    Article
  18. Article
  19. Review
  20. Review
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.

Thuy P DaoDepartments of Biology and Chemistry, Syracuse University, Syracuse, NY, 13244, USA.
Carlos A CastañedaDepartments of Biology and Chemistry, Syracuse University, Syracuse, NY, 13244, USA.ORCID 0000-0001-9634-0867
Syracuse University · US

Funding

The Role and Mechanisms of UBQLN2-mediated Phase Transitions in the Assembly and Disassembly of Biomolecular CondensatesR01GM136946 · NIGMS · SYRACUSE UNIVERSITY · PI CASTANEDA, CARLOS ANTONIO · 2020 to 2024
$1.5M
Amyotrophic Lateral Sclerosis Association 18-IIP-400Division of Molecular and Cellular BiosciencesNational Science Foundation 1750462NIGMS NIH HHS R01 GM136946
6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) has recently emerged as a possible mechanism that enables ubiquitin-binding shuttle proteins to facilitate the degradation of ubiquitinated substrates via distinct protein quality control (PQC) pathways. Shuttle protein LLPS is modulated by multivalent interactions among their various domains as well as heterotypic interactions with polyubiquitin chains. Here, the properties of three different shuttle proteins (hHR23B, p62, and UBQLN2) are closely examined, unifying principles for the molecular determinants of their LLPS are identified, and how LLPS is connected to their functions is discussed. Evidence supporting LLPS of other shuttle proteins is also found. In this review, it is proposed that shuttle protein LLPS leads to spatiotemporal regulation of PQC activities by mediating the recruitment of PQC machinery (including proteasomes or autophagic components) to biomolecular condensates, assembly/disassembly of condensates, selective enrichment of client proteins, and extraction of ubiquitinated proteins from condensates in cells.

Indexed as

ProteinsUbiquitinHumansProteasome Endopeptidase ComplexProteolysisProteasome Endopeptidase ComplexProteinsUbiquitinautophagybiomolecular condensatesliquid-liquid phase separationpolyubiquitinproteasomal degradationprotein quality controlubiquitin shuttle proteins

Identifiers

PMID32881044
PMCPMC7737676
OpenAlexW3083081718

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.