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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11110/20:10417620 RIV/00216208:11120/20:43920772

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Brain

ISSN

1756-6606

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

Nov 11

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

4

Strana od-do

149

Kód UT WoS článku

000590836700001

EID výsledku v databázi Scopus

2-s2.0-85095810865