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Article

Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism.

Nature communications - 1 Jul 2024

Heath Sarah G, Gray Shelby G, Hamzah Emilie M, O'Connor Karina M, Bozonet Stephanie M, Botha Alex D, de Cordovez Pierre, Magon Nicholas J, Naughton Jennifer D, Goldsmith Dylan L W, Schwartfeger Abigail J, Sunde Margaret, Buell Alexander K, Morris Vanessa K, Göbl Christoph

Abstract excerpt

The conversion of a soluble protein into polymeric amyloid structures is a process that is poorly understood. Here, we describe a fully redox-regulated amyloid system in which cysteine oxidation of the tumor suppressor protein p16INK4a leads to rapid amyloid formation. We identify a partially-structured disulfide-bonded dimeric intermediate species that subsequently assembles into fibrils. The stable amyloid...

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Identifiers

PMID: 38951545
DOI: 10.1038/s41467-024-49581-7
PMCID: PMC11217399

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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