Evidence map›Paper›PMID 27172186›Full record

ArticleG3 (Bethesda, Md.)2016

Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in Yeast.

Matthew J Maurer, Eric D Spear, Allen T Yu, Evan J Lee, Saba Shahzad, Susan Michaelis

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. A mutational atlas for Parkin proteostasis.Nature communications · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. HSP70-binding motifs function as protein quality control degrons.Cellular and molecular life sciences : CMLS · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Recognition and Degradation of Mislocalized Proteins in Health and Disease.Cold Spring Harbor perspectives in biology · 2019
    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

6 authors at 2 institutions in 1 country.

Matthew J MaurerDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Eric D SpearDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Allen T YuDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Evan J LeeDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Saba ShahzadDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Susan MichaelisDepartment of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 michaelis@jhmi.edu.
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

Trafficking of ABC proteins in yeastR01GM051508 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MICHAELIS, SUSAN D. · 1994 to 2010
$3.3M
NIGMS NIH HHS R01 GM051508
6 · The paper itself

Abstract

Cellular protein quality control (PQC) systems selectively target misfolded or otherwise aberrant proteins for degradation by the ubiquitin-proteasome system (UPS). How cells discern abnormal from normal proteins remains incompletely understood, but involves in part the recognition between ubiquitin E3 ligases and degradation signals (degrons) that are exposed in misfolded proteins. PQC is compartmentalized in the cell, and a great deal has been learned in recent years about ER-associated degradation (ERAD) and nuclear quality control. In contrast, a comprehensive view of cytosolic quality control (CytoQC) has yet to emerge, and will benefit from the development of a well-defined set of model substrates. In this study, we generated an isogenic "degron library" in Saccharomyces cerevisiae consisting of short sequences appended to the C-terminus of a reporter protein, Ura3 About half of these degron-containing proteins are substrates of the integral membrane E3 ligase Doa10, which also plays a pivotal role in ERAD and some nuclear protein degradation. Notably, some of our degron fusion proteins exhibit dependence on the E3 ligase Ltn1/Rkr1 for degradation, apparently by a mechanism distinct from its known role in ribosomal quality control of translationally paused proteins. Ubr1 and San1, E3 ligases involved in the recognition of some misfolded CytoQC substrates, are largely dispensable for the degradation of our degron-containing proteins. Interestingly, the Hsp70/Hsp40 chaperone/cochaperones Ssa1,2 and Ydj1, are required for the degradation of all constructs tested. Taken together, the comprehensive degron library presented here provides an important resource of isogenic substrates for testing candidate PQC components and identifying new ones.

Indexed as

ProteolysisAdenosine TriphosphatasesCytosolEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationGenes, ReporterHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsProteasome Endopeptidase ComplexProtein Sorting SignalsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein LigasesAdenosine TriphosphatasesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsLtn1 protein, S cerevisiaeProteasome Endopeptidase ComplexProtein Sorting SignalsRecombinant Fusion ProteinsRkr1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAN1 protein, S cerevisiaeSSA1 protein, S cerevisiaeSSA2 protein, S cerevisiaeSSM4 protein, S cerevisiaeUbiquitinUbiquitin-Protein LigasesUBR1 protein, S cerevisiaeURA3 protein, S cerevisiaeYDJ1 protein, S cerevisiaeE3 ligase Doa10Ltn1protein quality controlproteostasisubiquitin proteasome system

Identifiers

PMID27172186
PMCPMC4938640
OpenAlexW2350919937

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.