Evidence map›Paper›PMID 34827617›Full record

ArticleBiomolecules2021

The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites.

Rebeca Ibarra, Heather R Borror, Bryce Hart, Richard G Gardner, Gary Kleiger

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 7 citations in OpenAlex.

  1. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  2. 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

5 authors at 2 institutions in 1 country.

Rebeca IbarraDepartment of Chemistry and Biochemistry, University of Nevada, Las Vegas, NV 89154, USA.
Heather R BorrorDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Bryce HartDepartment of Chemistry and Biochemistry, University of Nevada, Las Vegas, NV 89154, USA.
Richard G GardnerDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Gary KleigerDepartment of Chemistry and Biochemistry, University of Nevada, Las Vegas, NV 89154, USA.ORCID 0000-0003-3924-1680
University of Nevada, Las Vegas · USUniversity of Washington · US

Funding

How ubiquitin-carrying enzymes contribute to ubiquitin ligase specificityR01GM141409 · NIGMS · UNIVERSITY OF NEVADA LAS VEGAS · PI KLEIGER, GARY L. · 2021 to 2024
$1.6M
Mechanisms for poly-ubiquitin chain initiation and elongationR15GM117555 · NIGMS · UNIVERSITY OF NEVADA LAS VEGAS · PI KLEIGER, GARY L. · 2015 to 2018
$785k
NIGMS NIH HHS R01 GM141409NIGMS NIH HHS R15 GM117555NIH HHS 1R01GM141409 - 01NIH HHS 2R15GM117555-02
6 · The paper itself

Abstract

Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome system. Here ubiquitin ligases must recognize and bind to misfolded proteins with sufficient energy to form a complex and with an adequate half-life to achieve poly-ubiquitin chain formation, the signal for protein degradation, prior to its dissociation from the ligase. It is not well understood how PQC ubiquitin ligases accomplish these tasks. Employing a fully reconstituted enzyme and substrate system to perform quantitative biochemical experiments, we demonstrate that the yeast PQC ubiquitin ligase San1 contains multiple substrate binding sites along its polypeptide chain that appear to display specificity for unique misfolded proteins. The results are consistent with a model where these substrate binding sites enable San1 to bind to misfolded substrates avidly, resulting in high affinity ubiquitin ligase-substrate complexes.

Indexed as

Protein FoldingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesBinding SitesProtein BindingSubstrate SpecificitySaccharomyces cerevisiae ProteinsSAN1 protein, S cerevisiaeUbiquitin-Protein Ligasesprotein degradationprotein quality controlubiquitin ligaseubiquitylation

Identifiers

PMID34827617
PMCPMC8615460
OpenAlexW3209020293

What Socratic 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 Socratic graph.