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T-type current modulation by the actin-binding protein Kelch-like 1.

K A Aromolaran¹, K A Benzow, L L Cribbs

¹Loyola University Chicago, Maywood, IL, USA.

American Journal of Physiology. Cell Physiology

|February 12, 2010

Summary

The neuronal actin-binding protein Kelch-like 1 (KLHL1) uniquely modulates T-type calcium currents by increasing the number of alpha(1H) channels, impacting cellular excitability.

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Area of Science:

Neuroscience
Molecular Biology
Cell Physiology

Background:

Neuronal actin-binding protein (ABP) Kelch-like 1 (KLHL1) is crucial for neuronal structure and function.
KLHL1 influences neurite outgrowth and upregulates P/Q-type calcium channel activity.
The role of KLHL1 in modulating low-voltage-gated calcium channels remains largely unexplored.

Purpose of the Study:

To investigate the role of KLHL1 as a modulator of T-type calcium channels.
To elucidate the molecular mechanism by which KLHL1 affects T-type calcium channel function.
To determine the specific subunits of T-type calcium channels regulated by KLHL1.

Main Methods:

Electrophysiology (including current density, calcium influx, noise analysis, and deactivation time measurements).
Biochemical assays (coexpression, immunoprecipitation, Western blot).
Cellular localization studies (immunolocalization in brain membrane fractions and HEK-293 cells).

Main Results:

Coexpression of KLHL1 with Ca(V)3.2 (alpha(1H) subunits) significantly increased T-type current density and calcium influx, but not with Ca(V)3.1 (alpha(1G)).
KLHL1 physically associates with alpha(1H) subunits, increasing the number of functional channels without altering single-channel conductance or open probability.
KLHL1 also increased the deactivation time of alpha(1H) currents, and this regulation was dependent on its actin-binding motif.

Conclusions:

KLHL1 represents a novel regulator of T-type calcium currents, specifically targeting the alpha(1H) subunit.
KLHL1 modulates alpha(1H) channel function by increasing channel number and altering deactivation kinetics, likely through interaction with both the channel and actin.
These findings highlight a new mechanism for controlling neuronal excitability and support KLHL1's broader role in neuronal function.