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ProteomicsUNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome
Myosin motors are critical for diverse motility functions ranging from cytokinesis and endocytosis to muscle contraction. The UNC-45 chaperone controls myosin function mediating the folding, assembly, and degradation of the muscle protein. Here, we analyze the molecular mechanism of UNC-45 as a hub ...
ORGANISM(S): Caenorhabditis elegans 
2024-07-25 | PXD040428 | Pride
Ufd-2 Myopathy Mhc-b Myo4 Protein quality control Crosslinking mass spectrometry Ubiquitin proteasome system Unc-45 Molecular chaperones Myosin proteostasis 
ProteomicsProteomics after labeling the vicinity of UNC-45 using miniTurbo and TurboID biotin ligases followed by streptavidin pull-down under non-stress and optogenetically induced mechanical muscle stress (OptIMMuS).
This project includes two proximity labeling experiments, one to establish the vicinity of UNC-45 under non-stress conditions and one to examine changes in the vicinity of UNC-45 under optogenetically induced mechanical muscle stress. The first non-stress experiment consists of 15 samples after biot...
ORGANISM(S): Caenorhabditis elegans 
2024-07-16 | PXD045081 | Pride
C. elegans Optogenetics Unc-45 Proximity labelling Mechanical stress Muscle 
UnknownThe UNC-45 myosin chaperone: from worms to flies to vertebrates.
Not available
S-EPMC4225561 | biostudies-literature
UnknownTracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.
Not available
S-EPMC3341559 | biostudies-literature
UnknownMolecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.
Not available
S-EPMC6803673 | biostudies-literature
UnknownThe UNC-45 chaperone mediates sarcomere assembly through myosin degradation in Caenorhabditis elegans.
Not available
S-EPMC2064129 | biostudies-literature
UnknownMyosin II co-chaperone general cell UNC-45 overexpression is associated with ovarian cancer, rapid proliferation, and motility.
Not available
S-EPMC2043524 | biostudies-literature
UnknownThe myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.
Not available
S-EPMC3549490 | biostudies-literature
UnknownX-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.
Not available
S-EPMC3060410 | biostudies-literature
UnknownUnc-45 mutations in Caenorhabditis elegans implicate a CRO1/She4p-like domain in myosin assembly.
Not available
S-EPMC2133068 | biostudies-literature
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