Novel ways to regulate T-type Ca<sup>2+</sup> channels

Peers, Chris; Elíes, Jacobo; Gamper, Nikita

doi:10.1080/19336950.2015.1017995

Cited by 1 publication

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“…7,8 Over the last few years, various pathways and mechanisms underlying the modulation of T-type channels have been identified. [9][10][11] Besides numerous small molecules that acutely modulate channel activity, 12 T-type channels are subject to regulation at the levels of transcription, [13][14][15] alternative splicing, [16][17][18][19] protein interaction, [20][21] and post-translational modification including ubiquitination 22 and phosphorylation. 23 In addition, asparagine (N)-linked glycosylation has emerged as an essential level of control of T-type channel expression.…”

Section: Introductionmentioning

confidence: 99%

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation

et al. 2016

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Low-voltage-gated T-type calcium channels are expressed throughout the nervous system where they play an essential role in shaping neuronal excitability. Defects in T-type channel expression have been linked to various neuronal disorders including neuropathic pain and epilepsy. Currently, little is known about the cellular mechanisms controlling the expression and function of T-type channels. Asparagine-linked glycosylation has recently emerged as an essential signaling pathway by which the cellular environment can control expression of T-type channels. However, the role of N-glycans in the conducting function of T-type channels remains elusive. In the present study, we used human Ca v 3.2 glycosylation-deficient channels to assess the role of N-glycosylation on the gating of the channel. Patch-clamp recordings of gating currents revealed that N-glycans attached to hCa v 3.2 channels have a minimal effect on the functioning of the channel voltage-sensor. In contrast, N-glycosylation on specific asparagine residues may have an essential role in the conducting function of the channel by enhancing the channel permeability and / or the pore opening of the channel. Our data suggest that modulation of N-linked glycosylation of hCa v 3.2 channels may play an important physiological role, and could also support the alteration of T-type currents observed in disease states.

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Section: Introductionmentioning

confidence: 99%

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation

et al. 2016

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Novel ways to regulate T-type Ca²⁺ channels

Cited by 1 publication

References 8 publications

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation

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Novel ways to regulate T-type Ca2+ channels

Cited by 1 publication

References 8 publications

Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation

Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation

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Novel ways to regulate T-type Ca²⁺ channels

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation

Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation