Keeping muscle cells fit: how one helper protein does the trick

The chaperone UNC45, crucial for muscle health, directs myosin—key for movement—toward removal or assembly pathways. The Clausen lab at the Research Institute of Molecular Pathology (IMP) revealed how this process is regulated, linking defects in myosin quality control to severe muscle diseases.

3D structure of myosin. The protein requires a set of molecular helpers–known as chaperones–to achieve its proper shape, such as the essential factor UNC45.

Chaperones are molecular machines that ensure all proteins in the cell acquire their correct shape. UNC45 is one such chaperone, an essential factor with a vital role in maintaining muscle health by ensuring myosin—a fundamental protein for muscle movement—remains in peak condition. It achieves this by directing faulty myosin toward removal pathways and healthy myosin toward assembly pathways. Researchers from Tim Clausen’s lab at the Research Institute of Molecular Pathology (IMP) have now revealed how the process is regulated, also shedding new light on how defects in myosin quality control can lead to severe muscle diseases. Their findings were published in the journal Nature Communications.

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