Research progress on the function of non-muscle myosin II during cell division

Figures

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  FIGURE 1. (A) Schematic diagram of the structural characteristics of myosin II. (B) Comparative table summarizing the differences in structure, function, and diseases caused by functional abnormalities between muscle myosin II and non-muscle myosin II.

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  FIGURE 2. NMII interacts with Actin after conformational transformation. In the presence of ATP, the unphosphorylated NMII folds into a tightly compressed conformation (incompetent NMII), where one head locks onto the other through asymmetric interactions, and its nonhelical tail also folds at these two points and interacts with the head to further compress protein molecules to impede myosin filament assembly. RLC phosphorylation disrupts head-head and head-tail interactions, turning the folded NMII (10S) into an elongated competent NMII (6S), resulting in the formation of NMII bipolar filaments in ionic strength under physiological conditions.

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  FIGURE 3. Effect of cell rounding defects on spindle formation and cell division. Cell division is accompanied by a series of drastic morphological changes, and the first step of cells entering mitotic prophase is to round into a spherical shape in morphology. The failure of cell rounding will lead to the abnormal division process and the generation of aneuploid daughter cells due to the insufficient space for assembly of the spindle.

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  FIGURE 4. Important associated proteins and protein complex involved in cleavage furrow hanging and ingression during cytokinesis.

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  FIGURE 5. Diseases associated with mutations or abnormalities of different Myosin proteins. (A) Human body schematic diagram indicating the body parts affected by different myosin gene mutations. (B) Table listing different myosin gene mutations and their corresponding diseases.