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• W2287727718 abstract "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 Cav3.2 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 hCav3.2 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 hCav3.2 channels may play an important physiological role, and could also support the alteration of T-type currents observed in disease states." @default.
• W2287727718 created "2016-06-24" @default.
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• W2287727718 date "2016-02-21" @default.
• W2287727718 modified "2023-10-14" @default.
• W2287727718 title "Modulation of Ca_v3.2 T-type calcium channel permeability by asparagine-linked glycosylation" @default.
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• W2287727718 doi "https://doi.org/10.1080/19336950.2016.1138189" @default.
• W2287727718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4954584" @default.
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• W2287727718 hasPublicationYear "2016" @default.
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