Functional identification of potential non-canonical N-glycosylation sites within Ca_v3.2 T-type calcium channels.

ABSTRACT: Low-voltage-activated T-type calcium channels are important contributors to nervous system function. Post-translational modification of these channels has emerged as an important mechanism to control channel activity. Previous studies have documented the importance of asparagine (N)-linked glycosylation and identified several asparagine residues within the canonical consensus sequence N-X-S/T that is essential for the expression and function of Ca_v3.2 channels. Here, we explored the functional role of non-canonical N-glycosylation motifs in the conformation N-X-C based on site directed mutagenesis. Using a combination of electrophysiological recordings and surface biotinylation assays, we show that asparagines N345 and N1780 located in the motifs NVC and NPC, respectively, are e

SUBMITTER: Ficelova V 

PROVIDER: S-EPMC7659234 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature