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.
Short Communication: Journal of Morphology and Anatomy
Short Communication: Journal of Morphology and Anatomy
Research Article: Journal of Morphology and Anatomy
Research Article: Journal of Morphology and Anatomy
Research Article: Journal of Morphology and Anatomy
Research Article: Journal of Morphology and Anatomy
Opinion: Journal of Morphology and Anatomy
Opinion: Journal of Morphology and Anatomy
Posters & Accepted Abstracts: Alternative & Integrative Medicine
Posters & Accepted Abstracts: Alternative & Integrative Medicine
Scientific Tracks Abstracts: Cancer Science & Therapy
Scientific Tracks Abstracts: Cancer Science & Therapy
Scientific Tracks Abstracts: Journal of Forensic Research
Scientific Tracks Abstracts: Journal of Forensic Research
Scientific Tracks Abstracts: Cancer Science & Therapy
Scientific Tracks Abstracts: Cancer Science & Therapy
Accepted Abstracts: Journal of Forensic Research
Accepted Abstracts: Journal of Forensic Research
Journal of Morphology and Anatomy received 63 citations as per Google Scholar report
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