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Article

Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.

Protein science : a publication of the Protein Society - 1 Nov 2021

Moncrief Taylor, Matheny Courtney J, Gaziova Ivana, Miller John M, Qadota Hiroshi, Benian Guy M, Oberhauser Andres F

Abstract excerpt

Proper muscle development and function depend on myosin being properly folded and integrated into the thick filament structure. For this to occur the myosin chaperone UNC-45, or UNC-45B, must be present and able to chaperone myosin. Here we use a combination of in vivo C. elegans experiments and in vitro biophysical experiments to analyze the effects of six missense mutations in conserved regions of...

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Identifiers

PMID: 34515376
DOI: 10.1002/pro.4180
PMCID: PMC8521276

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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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Mutations in conserved residues of the myosin chaperone UNC-45 result in both reduced stability and chaperoning activity.PMID 34515376Read ↗

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