Research can help solve this "chicken first" problem and determine a key protein that determines the size and firmness of myosin. Connectin is responsible for the kinetic and elasticity of muscles. It contains many independently folded protein domains, including repeated immunoglobulin-like (Ig) domains, that is, the protein is unfolded when stretched, and then folded when the tension is removed. A research team at the University of Arizona used a mouse model lacking the Ig domain of myosin to explore the effect of a small increase in myosin stiffness. The mutant mice showed slight curvature of the spine (often associated with skeletal muscle disorders), atrophy of soleus muscles in the legs, atrophy of the diaphragm, and changes in muscle contractions. The study found that increasing the stiffness of actin is the cause of the disease, not the result of pathological changes in skeletal muscle. Further investigation revealed that the increase in stiffness of actin was caused by excessive splicing factor RBM20 in mutant mice. The research results show that RMB20 plays a key role in determining the size and elasticity of myosin, so it may be a new target for the treatment of various muscle diseases.
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