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PMID: 17535809 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Selective inhibition of Cav3.3 T-type calcium channels by Galphaq/11-coupled muscarinic acetylcholine receptors.

The Journal of biological chemistry ·Vol. 282 ·No. 29 ·2007-07-20 ·Pages 21043-55

Hildebrand ME, David LS, Hamid J, Mulatz K, Garcia E, Zamponi GW, Snutch TP

Abstract

T-type calcium channels play critical roles in controlling neuronal excitability, including the generation of complex spiking patterns and the modulation of synaptic plasticity, although the mechanisms and extent to which T-type Ca(2+) channels are modulated by G-protein-coupled receptors (GPCRs) remain largely unexplored. To examine specific interactions between T-type Ca(2+) channel subtypes and muscarinic acetylcholine receptors (mAChRS), the Cav3.1 (alpha(1G)), Cav3.2 (alpha(1H)), and Cav3.3 (alpha) T-type Ca(2+)(1I)channels were co-expressed with the M1 Galpha(q/11)-coupled mAChR. Perforated patch recordings demonstrate that activation of M1 receptors has a strong inhibitory effect on Cav3.3 T-type Ca(2+) currents but either no effect or a moderate stimulating effect on Cav3.1 and Cav3.2 peak current amplitudes. This differential modulation was observed for both rat and human T-type Ca(2+) channel variants. The inhibition of Cav3.3 channels by M1 receptors is reversible, use-independent, and associated with a concomitant increase in inactivation kinetics. Loss-of-function experiments with genetically encoded antagonists of Galpha and Gbetagamma proteins and gain-of-function experiments with genetically encoded Galpha subtypes indicate that M1 receptor-mediated inhibition of Cav3.3 occurs through Galpha(q/11). This is supported by experiments showing that activation of the M3 and M5 Galpha(q/11)-coupled mAChRs also causes inhibition of Cav3.3 currents, although Galpha(i)-coupled mAChRs (M2 and M4) have no effect. Examining Cav3.1-Cav3.3 chimeric channels demonstrates that two distinct regions of the Cav3.3 channel are necessary and sufficient for complete M1 receptor-mediated channel inhibition and represent novel sites not previously implicated in T-type channel modulation.

MeSH Terms
Animals Biophysics/methods Calcium/metabolism Calcium Channels, T-Type/chemistry,metabolism Cell Line Electrophysiology GTP-Binding Protein alpha Subunits, Gq-G11/metabolism Humans Kinetics Membrane Transport Proteins/chemistry,metabolism Patch-Clamp Techniques Rats Receptors, Muscarinic/metabolism Signal Transduction Time Factors Transfection
Chemicals
CACNA1I protein, human Calcium Channels, T-Type Membrane Transport Proteins Receptors, Muscarinic GTP-Binding Protein alpha Subunits, Gq-G11 Calcium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Hildebrand Michael E
Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z4.
David Laurence S
Hamid Jawed
Mulatz Kirk
Garcia Esperanza
Zamponi Gerald W
Snutch Terrance P
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2007-07-20
Epub
2007-00-29
Pages
21043-55
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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