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Article

A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.

The Journal of biological chemistry - 6 Jul 2012

Theodoraki Maria A, Nillegoda Nadinath B, Saini Jagdeep, Caplan Avrom J

Abstract excerpt

Quality control ubiquitin ligases promote degradation of misfolded proteins by the proteasome. If the capacity of the ubiquitin/proteasome system is exceeded, then misfolded proteins accumulate in aggregates that are cleared by the autophagic system. To identify components of the ubiquitin/proteasome system that protect against aggregation, we analyzed a GFP-tagged protein kinase, Ste11ΔN(K444R)-GFP, in yeast...

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Source

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Identifiers

PMID: 22593585
DOI: 10.1074/jbc.M112.341164
PMCID: PMC3390667

Genes

UBR1
LTN1
UBR2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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