Regulation of localization and function of L-type calcium channels by junctophilins

2022 ◽  
Vol 157 (1) ◽  
pp. 4-8
Author(s):  
Tsutomu Nakada ◽  
Mitsuhiko Yamada
Keyword(s):  
Calcium Channels ◽  
And Function

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

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Vendula Ficelova ◽  
Ivana A. Souza ◽  
Leos Cmarko ◽  
Maria A. Gandini ◽  
Robin N. Stringer ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Calcium Channels ◽  
Low Voltage ◽  
Consensus Sequence ◽  
Site Directed Mutagenesis ◽  
Post Translational Modification ◽  
Functional Identification ◽  
Electrophysiological Recordings ◽  
Nervous System Function ◽  
And Function

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 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.

Voltage-Gated Calcium Channels: Structure and Function (CACNA)

2012 ◽  
pp. 1984-1992
Author(s):  
Marta Vázquez-Cedeira ◽  
Diana M. Monsalve ◽  
Marta Sanz-García ◽  
Pedro A. Lazo ◽  
Thierry Galli ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Structure And Function ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
And Function

Structure and Function of Voltage-Dependent Calcium Channels from Muscle

1993 ◽  
Vol 707 (1 Molecular Bas) ◽  
pp. 81-86 ◽  
Author(s):  
TSUTOMU TANABE ◽  
ATSUSHI MIKAMI ◽  
TETSUHIRO NIIDOME ◽  
SHOSAKU NUMA ◽  
BRETT A. ADAMS ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Structure And Function ◽  
Voltage Dependent ◽  
Voltage Dependent Calcium Channels ◽  
And Function

scholarly journals Voltage-Gated Calcium Channels Exist and Function as Fragment-Channels in Neuronal Plasma Membranes

2013 ◽  
Vol 104 (2) ◽  
pp. 462a
Author(s):  
Ioannis E. Michailidis ◽  
Kathryn Abele ◽  
Wei K. Zhang ◽  
Lawrence Geyman ◽  
Bochao Lin ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Plasma Membranes ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
And Function

scholarly journals Rab11-dependent recycling of calcium channels is mediated by auxiliary subunit α2δ-1 but not α2δ-3

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
James O. Meyer ◽  
Annette C. Dolphin
Keyword(s):  
Plasma Membrane ◽  
Calcium Channels ◽  
Dominant Negative ◽  
Calcium Currents ◽  
Dependent Manner ◽  
Auxiliary Subunit ◽  
Voltage Gated Calcium Channels ◽  
Endosomal Recycling ◽  
Recycling Pathway ◽  
And Function

AbstractN-type voltage-gated calcium channels (CaV2.2) are predominantly expressed at presynaptic terminals, and their function is regulated by auxiliary α2δ and β subunits. All four mammalian α2δ subunits enhance calcium currents through CaV1 and CaV2 channels, and this increase is attributed, in part, to increased CaV expression at the plasma membrane. In the present study we provide evidence that α2δ-1, like α2δ-2, is recycled to the plasma membrane through a Rab11a-dependent endosomal recycling pathway. Using a dominant-negative Rab11a mutant, Rab11a(S25N), we show that α2δ-1 increases plasma membrane CaV2.2 expression by increasing the rate and extent of net forward CaV2.2 trafficking in a Rab11a-dependent manner. Dominant-negative Rab11a also reduces the ability of α2δ-1 to increase CaV2.2 expression on the cell-surface of hippocampal neurites. In contrast, α2δ-3 does not enhance rapid forward CaV2.2 trafficking, regardless of whether Rab11a(S25N) is present. In addition, whole-cell CaV2.2 currents are reduced by co-expression of Rab11a(S25N) in the presence of α2δ-1, but not α2δ-3. Taken together these data suggest that α2δ subtypes participate in distinct trafficking pathways which in turn influence the localisation and function of CaV2.2.

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