Increase of CaV3 channel activity induced by HVA β1b-subunit is not mediated by a physical interaction

Objective Low voltage-activated (LVA) calcium channels are crucial for regulating oscillatory behavior in several types of neurons and other excitable cells. LVA channels dysfunction has been implicated in epilepsy, neuropathic pain, cancer, among other diseases. Unlike for High Voltage-Activated (H...

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Published in:BMC research notes 2018-11, Vol.11 (1), p.1-810, Article 810
Main Authors: Arteaga-Tlecuitl, Rogelio, Sanchez-Sandoval, Ana Laura, Ramirez-Cordero, Belen Ernestina, Rosendo-Pineda, Margarita Jacaranda, Vaca, Luis, Gomora, Juan Carlos
Format: Article
Language:English
Subjects:
Calcium channels
Calcium channels (voltage-gated)
Cancer
CaV3 channel
Channel gating
Cloning
Confocal microscopy
Electrophysiology
Epilepsy
Fluorescence
Gene expression
Immunoprecipitation
Kinetics
Neuralgia
Proteins
Protein–protein interaction
Research Note
Voltage-gated calcium channel
Western blotting
β-Subunit
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Summary:Objective Low voltage-activated (LVA) calcium channels are crucial for regulating oscillatory behavior in several types of neurons and other excitable cells. LVA channels dysfunction has been implicated in epilepsy, neuropathic pain, cancer, among other diseases. Unlike for High Voltage-Activated (HVA) channels, voltage-dependence and kinetics of currents carried by recombinant LVA, i.e., CaV3 channels, are quite similar to those observed in native currents. Therefore, whether these channels are regulated by HVA auxiliary subunits, remain controversial. Here, we used the α1-subunits of CaV3.1, CaV3.2, and CaV3.3 channels, together with HVA auxiliary β-subunits to perform electrophysiological, confocal microscopy and immunoprecipitation experiments, in order to further explore this possibility. Results Functional expression of CaV3 channels is up-regulated by all four β-subunits, although most consistent effects were observed with the β1b-subunit. The biophysical properties of CaV3 channels were not modified by any β-subunit. Furthermore, although β1b-subunits increased colocalization of GFP-tagged CaV3 channels and the plasma membrane of HEK-293 cells, western blots analysis revealed the absence of physical interaction between CaV3.3 and β1b-subunits as no co-immunoprecipitation was observed. These results provide solid evidence that the up-regulation of LVA channels in the presence of HVA-β1b subunit is not mediated by a high affinity interaction between both proteins.
ISSN:1756-0500
1756-0500
DOI:10.1186/s13104-018-3917-1