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Article

Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.

Nature communications - 21 Oct 2019

Hellerschmied Doris, Lehner Anita, Franicevic Nina, Arnese Renato, Johnson Chloe, Vogel Antonia, Meinhart Anton, Kurzbauer Robert, Deszcz Luiza, Gazda Linn, Geeves Michael, Clausen Tim

Abstract excerpt

Myosin is a motor protein that is essential for a variety of processes ranging from intracellular transport to muscle contraction. Folding and assembly of myosin relies on a specific chaperone, UNC-45. To address its substrate-targeting mechanism, we reconstitute the interplay between Caenorhabditis elegans UNC-45 and muscle myosin MHC-B in insect cells. In addition to providing a cellular chaperone assay, the...

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Identifiers

PMID: 31636255
DOI: 10.1038/s41467-019-12667-8
PMCID: PMC6803673

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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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