Septin Phosphorylation

Septins are a class of GTP-binding proteins that are conserved across many eukaryotes. Individual septin interacts with each other and interacts with various heteromeric structures that form filters and structures of high order in vivo. The mechanisms underlying the assembly and maintenance of structures with high order in cells are poorly understood. Septins in several species have been shown to be phosphorylated, although it is precisely how septin phosphorylation may contribute to the formation of high-throughput septin structures. Four septins were activated by a full-blown fungus, Ashbya gossypii, phosphorylated, and show here the various roles of these phosphorylation sites in septin ring formation and septin dynamics, as well as cell morphology and efficiency.

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