Key result
UNC-45a functions as a myosin chaperone in vivo, and its absence leads to severe defects in stress fiber assembly, cell morphogenesis, polarity, and migration.
UNC-45a functions as a critical myosin chaperone in vivo, promoting the generation of contractile actomyosin bundles through synchronized NM-II folding and filament-assembly activities.
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UNC-45a is essential for stress fiber assembly; hypothesis-generating for myosin regulation but leaves open any cardiovascular translation.
Lehtimäki et al. (2017) studied this question. UNC-45a knockout was evaluated on Stress fiber assembly and nonmuscle myosin II (NM-II) folding. UNC-45a functions as a myosin chaperone in vivo, and its absence leads to severe defects in stress fiber assembly, cell morphogenesis, polarity, and migration.
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