Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly.

doi:10.1083/jcb.143.5.1215

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Article

Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly.

The Journal of cell biology - 30 Nov 1998

Barral J M, Bauer C C, Ortiz I, Epstein H F

Abstract excerpt

The Caenorhabditis elegans unc-45 locus has been proposed to encode a protein machine for myosin assembly. The UNC-45 protein is predicted to contain an NH2-terminal domain with three tetratricopeptide repeat motifs, a unique central region, and a COOH-terminal domain homologous to CRO1 and She4p...

Topics

Alleles
Amino Acid Sequence
Animals
Base Sequence
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Cytoskeletal Proteins
DNA Primers
Fungal Proteins
Genes, Helminth
Microscopy, Electron
Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Myosins

Phenotype

Polymerase Chain Reaction

Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 9832550
DOI: 10.1083/jcb.143.5.1215
PMCID: PMC2133068

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9832550-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Unc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly.PMID 9832550Read ↗

The UCS family of myosin chaperonesSemantic proximity Read ↗

The UNC-45 myosin chaperone: from worms to flies to vertebrates.Semantic proximity Read ↗

Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegansSemantic proximity Read ↗

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

Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans.Semantic proximity Read ↗

The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegans.Semantic proximity Read ↗

Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.Semantic proximity Read ↗

Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival.Semantic proximity Read ↗

Pathogenic Variants in the Myosin Chaperone UNC-45B Cause Progressive Myopathy with Eccentric Cores.Semantic proximity Read ↗

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

The myosin co-chaperone UNC-45 is required for skeletal and cardiac muscle function in zebrafish.Semantic proximity Read ↗

The unc-45 gene of Caenorhabditis elegans is an essential muscle-affecting gene with maternal expression.Semantic proximity Read ↗

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