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Article

Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis.

Molecular and cellular biology - 1 Nov 2003

Meriin Anatoli B, Zhang Xiaoqian, Miliaras Nicholas B, Kazantsev Alex, Chernoff Yury O, McCaffery J Michael, Wendland Beverly, Sherman Michael Y

Abstract excerpt

The role of aggregation of abnormal proteins in cellular toxicity is of general importance for understanding many neurological disorders. Here, using a yeast model, we demonstrate that mutations in many proteins involved in endocytosis and actin function dramatically enhance the toxic effect of polypeptides with an expanded polyglutamine (polyQ) domain. This enhanced cytotoxicity required polyQ aggregation and...

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Identifiers

PMID: 14560003
DOI: 10.1128/MCB.23.21.7554-7565.2003
PMCID: PMC207640

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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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