Septin Phosphorylation | Open Access Journals

Journal of Morphology and Anatomy

ISSN: 2684-4265

Open Access

Septin Phosphorylation

Septins are a class of GTP-binding proteins conserved throughout many eukaryotes. Individual septin subunits associate with one another 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 have been shown to be phosphorylated, although precisely how septin phosphorylation may be contributing to the formation of high-order septin structures is unknown. SEPT12 is phosphorylated via Protein kinase A (PKA), and its phosphorylation interfered with SEPT12 polymerization into complexes and filaments. Taken together, the phosphorylation status of SEPT12 is crucial for its function in regulating the mammalian sperm physiology.

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