Alpha-actinin was first identified in 1964 by Setsuro and Fumiko Ebashi in a biochemical fraction from muscle that promoted actomyosin contraction (Ebashi et al. 1964). However, it was experiments that they performed with Koscak Maruyama that defined what is now regarded as the primary function of alpha-actinin, namely, the cross-linking of actin filaments. This cross-linking ability was observed in vitro as the formation of gels when alpha-actinin was mixed with F-actin, while bundling of actin filaments was observed by electron microscopy. The name alpha-actinin was Maruyama’s suggestion, with another factor that he had identified and characterized being designated beta-actinin. Beta-actinin is unrelated to alpha-actinin and is now almost exclusively called Cap Z, or capping protein, reflecting its function in the Z-disk of the muscle sarcomere where it caps the barbed (+) end of actin filaments. Thus...
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