Proper phosphorylation of septin 12 regulates septin 4 and soluble adenylyl cyclase expression to induce sperm capacitation

Author:

Wang Han‐Yu12,Shen Yi‐Ru2,Tsai Yung‐Chieh3,Wu Shang‐Rung4,Wang Chia‐Yih15ORCID,Kuo Pao‐Lin16ORCID

Affiliation:

1. Institute of Basic Medical Sciences, College of Medicine National Cheng Kung University Tainan Taiwan

2. Department of Obstetrics and Gynecology, College of Medicine National Cheng Kung University Tainan Taiwan

3. Department of Obstetrics and Gynecology, Sport Management, and Biotechnology, Chi‐Mei Medical Center Chia Nan University of Pharmacy and Science Tainan Taiwan

4. Institute of Oral Medicine, College of Medicine National Cheng Kung University Tainan Taiwan

5. Department of Cell Biology and Anatomy, College of Medicine National Cheng Kung University Tainan Taiwan

6. Department of Obstetrics and Gynecology, National Cheng Kung University Hospital, College of Medicine National Cheng Kung University Tainan Taiwan

Abstract

AbstractSeptin‐based ring complexes maintain the sperm annulus. Defective annular structures are observed in the sperm of Sept12‐ and Sept4‐null mice. In addition, sperm capacitation, a process required for proper fertilization, is inhibited in Sept4‐null mice, implying that the sperm annulus might play a role in controlling sperm capacitation. Hence, we analyzed sperm capacitation of sperm obtained from SEPT12 Ser196 phosphomimetic (S196E), phosphorylation‐deficient (S196A), and SEPT4‐depleted mutant mice. Capacitation was reduced in the sperm of both the Sept12 S196E‐ and Sept12 S196A‐knock‐in mice. The protein levels of septins, namely, SEPT4 and SEPT12, were upregulated, and these proteins were concentrated in the sperm annulus during capacitation. Importantly, the expression of soluble adenylyl cyclase (sAC), a key enzyme that initiates capacitation, was upregulated, and sAC was recruited to the sperm annulus following capacitation stimulation. We further found that SEPT12, SEPT4, and sAC formed a complex and colocalized to the sperm annulus. Additionally, sAC expression was reduced and disappeared in the annulus of the SEPT12 S196E‐ and S196A‐mutant mouse sperm. In the sperm of the SEPT4‐knockout mice, sAC did not localize to the annulus. Thus, our data demonstrate that SEPT12 phosphorylation status and SEPT4 activity jointly regulate sAC protein levels and annular localization to induce sperm capacitation.

Funder

Ministry of Science and Technology

Publisher

Wiley

Subject

Cell Biology,Clinical Biochemistry,Physiology

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