Journal of Biochemistry Research

Septin Phosphorylation

Septins are a category of GTP-binding proteins conserved throughout many eukaryotes. Individual septin subunits accompany each other and assemble into heteromeric complexes that form filaments and higher-order structures in vivo . The mechanisms underlying the assembly and maintenance of higher-order structures in cells remain poorly understood. Septins in several organisms are shown to be phosphorylated, although precisely how septin phosphorylation could also be contributing to the formation of high-order septin structures is unknown. Four of the five septins expressed within the filamentous fungus, Ashbya gossypii, are phosphorylated, and that we demonstrate here the various roles of those phosphorylation sites in septin ring formation and septin dynamics, also as cell morphology and viability.    

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