Functional identification of potential non-canonical N-glycosylation sites within Cav3.2 T-type calcium channels

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00534943" target="_blank" >RIV/61388963:_____/20:00534943 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11110/20:10417620 RIV/00216208:11120/20:43920772
Result on the web
<a href="https://doi.org/10.1186/s13041-020-00697-z" target="_blank" >https://doi.org/10.1186/s13041-020-00697-z</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1186/s13041-020-00697-z" target="_blank" >10.1186/s13041-020-00697-z</a>

Result language
angličtina
Original language name
Functional identification of potential non-canonical N-glycosylation sites within Cav3.2 T-type calcium channels
Original language description
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 Cav3.2 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 essential for the expression of the human Cav3.2 channel in the plasma membrane. Therefore, these newly identified asparagine residues within non-canonical motifs add to those previously reported in canonical sites and suggest that N-glycosylation of Cav3.2 may also occur at non-canonical motifs to control expression of the channel in the plasma membrane. It is also the first study to report the functional importance of non-canonical N-glycosylation motifs in an ion channel.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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