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Article

Mutations in Hsp40 co-chaperone change the canonical interdomain interactions stimulating LGMDD1 myopathy.

The Journal of biological chemistry - 1 Jan 2026

Bhadra Ankan K, Aggarwal Geetika, Jaysingh Anshuman, Chen Daniel, Daw Jil, Weihl Conrad C, True Heather L

Abstract excerpt

Limb-girdle muscular dystrophy D1 (LGMDD1) is a rare, dominantly inherited neuromuscular protein-misfolding chaperonopathy caused by mutations in the Hsp40 co-chaperone DNAJB6, primarily in the glycine-phenylalanine (GF) or J-domains. Currently, no treatments are available, and a challenge in understanding the disease is identifying a specific client protein for DNAJB6 in skeletal muscle. DNAJB6 has homology to...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 41241098
DOI: 10.1016/j.jbc.2025.110945
PMCID: PMC12756002

Genes

DNAJB6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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Mutations in Hsp40 co-chaperone change the canonical interdomain interactions stimulating LGMDD1 myopathy.PMID 41241098Read ↗

Mutations in Hsp40 co-chaperone change the unique canonical inter-domain interactions stimulating LGMDD1 myopathySemantic proximity Read ↗

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