Evidence map›Paper›PMID 35357021›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2022

A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.

Jacob A Culver, Xia Li, Matthew Jordan, Malaiyalam Mariappan

Open access · greenAbstract readReviewVideo-Audio Media
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Frontiers in molecular biosciences · 2023
    Article
  8. 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

4 authors at 1 institution in 1 country.

Jacob A CulverDepartment of Cell Biology, Nanobiology Institute, Yale School of Medicine, Yale University West Campus, West Haven, Connecticut, USA.
Xia LiDepartment of Cell Biology, Nanobiology Institute, Yale School of Medicine, Yale University West Campus, West Haven, Connecticut, USA.
Matthew JordanDepartment of Cell Biology, Nanobiology Institute, Yale School of Medicine, Yale University West Campus, West Haven, Connecticut, USA.
Malaiyalam MariappanDepartment of Cell Biology, Nanobiology Institute, Yale School of Medicine, Yale University West Campus, West Haven, Connecticut, USA.ORCID 0000-0002-2966-1182
Yale University · US

Funding

The mechanism of Ire1-mediated mRNA cleavage during endoplasmic reticulum stressR01GM117386 · NIGMS · YALE UNIVERSITY · PI MARIAPPAN, MALAIYALAM · 2016 to 2024
$3.0M
NIGMS NIH HHS R01 GM117386
6 · The paper itself

Abstract

Molecular chaperones in cells constantly monitor and bind to exposed hydrophobicity in newly synthesized proteins and assist them in folding or targeting to cellular membranes for insertion. However, proteins can be misfolded or mistargeted, which often causes hydrophobic amino acids to be exposed to the aqueous cytosol. Again, chaperones recognize exposed hydrophobicity in these proteins to prevent nonspecific interactions and aggregation, which are harmful to cells. The chaperone-bound misfolded proteins are then decorated with ubiquitin chains denoting them for proteasomal degradation. It remains enigmatic how molecular chaperones can mediate both maturation of nascent proteins and ubiquitination of misfolded proteins solely based on their exposed hydrophobic signals. In this review, we propose a dynamic ubiquitination and deubiquitination model in which ubiquitination of newly synthesized proteins serves as a "fix me" signal for either refolding of soluble proteins or retargeting of membrane proteins with the help of chaperones and deubiquitinases. Such a model would provide additional time for aberrant nascent proteins to fold or route for membrane insertion, thus avoiding excessive protein degradation and saving cellular energy spent on protein synthesis. Also see the video abstract here: https://youtu.be/gkElfmqaKG4.

Indexed as

Molecular ChaperonesProtein FoldingProtein TransportUbiquitinUbiquitinationMolecular ChaperonesUbiquitinchaperonesdeubiquitinationprotein foldingprotein misfoldingprotein quality controlprotein unfoldingtail-anchored proteinsubiquitination

Identifiers

PMID35357021
PMCPMC9133216
OpenAlexW4220698217

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.