Cofilin-1 Protein, Human (His)

Cofilin-1 protein exhibits pH-sensitive F-actin depolymerizing activity by binding to F-actin. In collaboration with the subcortical maternal complex (SCMC), it plays a crucial role in enabling zygotes to progress beyond the initial embryonic cell divisions through the regulation of actin dynamics. Additionally, Cofilin-1 is essential for the centralization of the mitotic spindle and symmetric division of zygotes. In epithelial cells, it contributes to the regulation of cell morphology and cytoskeletal organization. Furthermore, Cofilin-1 is required for the up-regulation of the atypical chemokine receptor ACKR2, facilitating its efficient translocation from endosomal compartments to the cell membrane, thereby enhancing chemokine uptake and degradation. Its involvement extends to neural tube morphogenesis and neural crest cell migration. Functionally, Cofilin-1 can bind G- and F-actin in a 1:1 ratio, constituting a major component of intranuclear and cytoplasmic actin rods. Interactions with the subcortical maternal complex involve TLE6 isoform 1 and NLRP5, along with interaction with C9orf72.