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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Leptin activation of ATP-sensitive K+ (KATP) channels in rat CRI-G1 insulinoma cells involves disruption of the actin

J Harvey¹, S C Hardy, A J Irving

¹Department of Biomedical Sciences, Institute of Medical Sciences, Aberdeen Centre for Energy Regulation and Obesity, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.

The Journal of Physiology

|August 16, 2000

Summary

Leptin activates ATP-sensitive K+ (KATP) channels by disrupting actin filaments in insulin-secreting cells. This process involves phosphoinositide 3-kinase and actin cytoskeleton remodeling, not microtubules.

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Area of Science:

Cell Biology
Molecular Physiology
Endocrinology

Background:

ATP-sensitive K+ (KATP) channels play a crucial role in insulin secretion.
Leptin, a hormone regulating appetite and metabolism, influences insulin secretion.
The cytoskeleton's role in leptin's effect on KATP channels is not fully understood.

Purpose of the Study:

To investigate the involvement of the cytoskeleton in leptin-induced KATP channel activation.
To elucidate the specific cytoskeletal components and signaling pathways mediating this effect.

Main Methods:

Patch clamp electrophysiology to measure KATP channel activity.
Fluorescence imaging with rhodamine-conjugated phalloidin to visualize actin filaments.
Application of specific cytoskeleton-disrupting and stabilizing agents.

Main Results:

Phalloidin, an actin stabilizer, blocked leptin-induced KATP channel activation.
Actin destabilizers (DNase 1, cytochalasin B) increased KATP channel activity.
Leptin induced rapid actin filament disassembly, mediated by phosphoinositide 3-kinase (PI 3-kinase).
Anti-microtubule agents did not affect KATP channel activity.

Conclusions:

Leptin activates KATP channels in insulin-secreting cells via actin cytoskeleton disruption.
PI 3-kinase signaling is essential for leptin-induced actin remodeling and KATP channel activation.
The findings highlight a novel mechanism linking leptin signaling, actin dynamics, and ion channel function.