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Article

The ALS-associated E425K mutation uncouples DNAJC7 from the Hsp70 chaperone cycle.

The FEBS journal - 1 Jun 2026

Elmaleh Bar, Faust Ofrah, Rosenzweig Rina

Abstract excerpt

DNAJC7, a member of the J-domain protein (JDP/Hsp40) family, plays a key role in protein homeostasis by regulating Hsp70 activity and preventing protein aggregation. Mutations in DNAJC7 have been linked to amyotrophic lateral sclerosis (ALS); yet, the molecular mechanisms by which these variants impair chaperone function remain poorly understood. DNAJC7 is a conserved chaperone featuring both a canonical...

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Source

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Identifiers

PMID: 41531269
DOI: 10.1111/febs.70395
PMCID: PMC13278355

Genes

DNAJC7
TPR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

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