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Related Experiment Video

Updated: Dec 17, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

The Slo3/Lrrc52 complex is sensitive to phosphoinositides.

Takafumi Kawai¹, Yasushi Okamura^1,2

¹Graduate School of Medicine, Osaka University , Suita, Japan.

Channels (Austin, Tex.)

|June 23, 2020

Summary

Voltage-sensing phosphatase (VSP) regulates sperm-specific potassium (K+) channels (Slo3) activity. VSP

Area of Science:

Biochemistry
Molecular Biology
Cell Physiology

Background:

Voltage-sensing phosphatase (VSP) exhibits voltage-dependent phosphatase activity towards phosphoinositides.
VSP activation generates polarized phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) distribution in sperm flagella, influencing sperm-specific potassium (K+) channel Slo3 activity.
The auxiliary subunit Lrrc52 significantly alters the electrophysiological properties of Slo3.

Purpose of the Study:

To investigate the regulation of Slo3 channel activity by VSP in the presence of its auxiliary subunit, Lrrc52.
To analyze the PtdIns(4,5)P2-dependence of Slo3 activity in a heterologous expression system with Lrrc52.
To confirm the role of VSP in regulating Slo3 activity in a heterologous system, mirroring its function in native sperm.

Main Methods:

Keywords:

Lrrc52 PIPs Slo3

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

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Published on: October 15, 2016

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Last Updated: Dec 17, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

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Published on: March 14, 2021

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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

Utilized *Xenopus* oocytes as a heterologous expression system.
Co-expressed VSP, Slo3, and Lrrc52 in *Xenopus* oocytes.
Analyzed the electrophysiological properties and VSP-dependent regulation of Slo3-Lrrc52 complex.

Main Results:

Slo3 co-expressed with Lrrc52 maintained similar sensitivity to VSP activity as Slo3 alone.
VSP effectively regulated the activity of the Slo3-Lrrc52 complex in *Xenopus* oocytes.
These findings indicate that Lrrc52 does not abolish VSP's regulatory effect on Slo3.

Conclusions:

VSP regulates the activity of the Slo3-Lrrc52 complex in a manner consistent with its regulation of Slo3 alone.
This study supports the previous findings that VSP plays a role in regulating Slo3 activity within the native sperm flagellum.
The results highlight the conserved mechanism of VSP-Slo3 interaction across different expression systems.