ATP hydrolysis provides energy for actomyosin contraction. Adding ATP to a mixture of both proteins (called actomyosin) causes a decrease in viscosity. Lat-A-induces reduction of actomyosin contractility. The specificity of zingibain's binding ensures predominant hydrolyzation of actomyosin and Type I collagen. It is composed of actin and myosin II bundles, thus the term actomyosin. The source of cytoskeletal traction is actomyosin contractility. In plant cells, there is no actomyosin ring. A retained the original name, whereas they renamed myosin B as actomyosin. This technique allowed him to precipitate actomyosin components together with the desired proteins. In humans, the main function of ROCK1 is actomyosin contractility. In muscle cells, actomyosin myofibrils makeup much of the cytoplasmic material. The ectoplasm owes its highly viscous state, in part, to the cross-linking actomyosin complex. In molecular biology, an actomyosin contractile ring is a prominent structure during cytokinesis. Additionally, it is hypothesized that anillin couples the actomyosin cytoskeleton to microtubules by binding MgcRacGAP/CYK-4/RacGAP50C. These actomyosin rings invaginate to separate all nuclei for one another in the syncytial blastoderm.