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Related Experiment Video

Updated: Jul 13, 2026

Real-Time Imaging of Acrosomal Calcium Dynamics and Exocytosis in Live Mouse Sperm

Real-Time Imaging of Acrosomal Calcium Dynamics and Exocytosis in Live Mouse Sperm

Published on: October 13, 2023

Complexin/synaptotagmin interplay controls acrosomal exocytosis.

Carlos M Roggero¹, Gerardo A De Blas, Han Dai

¹Laboratorio de Biología Celular y Molecular, Instituto de Histología y Embriología (IHEM-CONICET), Facultad de Ciencias Médicas, Universidad Nacional de Cuyo, Mendoza 5500, Argentina.

The Journal of Biological Chemistry

|July 7, 2007

Summary

This study reveals that complexin and synaptotagmin VI interaction regulates sperm acrosomal exocytosis. Phosphorylation of synaptotagmin VI

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Area of Science:

Cellular Biology
Molecular Biology
Reproductive Biology

Background:

Regulated secretion is vital for cell function, with acrosomal exocytosis in sperm crucial for fertilization.
SNARE proteins, synaptotagmin I, and complexin are key regulators of secretion.
The precise roles of complexin and synaptotagmin in non-neuronal secretion remain unclear.

Purpose of the Study:

To investigate the interplay between complexin and synaptotagmin VI in human sperm acrosomal exocytosis.
To determine the impact of synaptotagmin VI C2B domain and complexin on SNARE complex formation and fusion.
To explore the modulatory role of phosphorylation on synaptotagmin VI function in secretion.

Main Methods:

Utilized permeabilized human sperm models to study exocytosis.
Employed synaptotagmin VI C2B domain and anti-complexin antibodies to probe protein interactions.
Investigated the effects of complexin and synaptotagmin VI C2B domain on SNARE complex assembly and exocytosis progression.
Introduced phosphomimetic mutations in the synaptotagmin VI C2B domain to assess functional consequences.

Main Results:

The synaptotagmin VI C2B domain and anti-complexin antibody inhibited trans SNARE complex formation, an effect reversed by complexin.
Excess complexin blocked exocytosis at a later stage, after SNARE complex assembly, which was rescued by the synaptotagmin VI C2B domain in a Ca(2+)-dependent manner.
A phosphomimetic mutation in the synaptotagmin VI C2B domain impaired Ca(2+) and phospholipid binding, abolishing its ability to rescue the complexin-induced block.

Conclusions:

The functional interplay between complexin and synaptotagmin VI is critical for regulating physiological sperm acrosomal exocytosis.
Synaptotagmin VI's C2B domain, modulated by phosphorylation, plays a key role in controlling the fusion process.
This study provides direct evidence for the complexin/synaptotagmin interplay in a non-neuronal secretory system, highlighting potential phosphorylation-dependent regulation.