Glycosylation of voltage-gated calcium channels in health and disease.

  title={Glycosylation of voltage-gated calcium channels in health and disease.},
  author={Joanna Lazniewska and Norbert Weiss},
  journal={Biochimica et biophysica acta. Biomembranes},
  volume={1859 5},

The life cycle of voltage-gated Ca2+ channels in neurons: an update on the trafficking of neuronal calcium channels

The current evidence concerning the regulatory mechanisms which underlie precise control of neuronal CaV channel trafficking are addressed and their potential as therapeutic targets are discussed.

T-type calcium channels: From molecule to therapeutic opportunities.

Cell glycosaminoglycans content modulates human voltage‐gated proton channel (HV1) gating

Evidence is presented that mechanosensitivity of the dimeric HV1 channel transduce changes on cell membrane fluidity related to the defective biosynthesis of chondroitin sulfate and heparan sulfate in Chinese Hamster Ovary cells into a leftward shift in the activation voltage dependence.

Genetic T-type calcium channelopathies

The genetics of T-type channels are presented with an emphasis on structure-function relationships and associated channelopathies, including epilepsy, autism spectrum disorders, schizophrenia, motor neuron disorders and aldosteronism.

N-Glycosylation of TREK-1/hK2P2.1 Two-Pore-Domain Potassium (K2P) Channels

It is demonstrated that nonglycosylated hTREK-1 channel subunits are able to reach the cell surface in general but with seemingly reduced efficiency compared to glycosylation-deficient subunits.

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

Asparagines N345 and N1780 located in the motifs NVC and NPC, respectively, are essential for the expression of the human Ca v 3.2 channel in the plasma membrane and are reported in the first study to report the functional importance of non-canonical N-glycosylation motifs in an ion channel.

Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels

The present study reveals that glycosylation is an indispensable determinant of the modulation of β1-subunit on BK channel pharmacology and its activation, and could lead to the dysfunction of Bk channel, resulting in a pathological state.

Eukaryotic Voltage-Gated Sodium Channels: On Their Origins, Asymmetries, Losses, Diversification and Adaptations

The appearance of voltage-gated, sodium-selective channels with rapid gating kinetics was a limiting factor in the evolution of nervous systems andMulticellularity and the appearance of systems was an impetus for Nav1 channels to adapt to sodium ion selectivity and fast ion gating.



The "sweet" side of ion channels.

The discovery of detailed mechanisms of regulation of ions channels by glycosylation provides new insights in the physiology of ion channels and may allow developing new pharmaceutics for the treatment of ion channel-related disorders.

Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation

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.

G Protein Regulation of Neuronal Calcium Channels: Back to the Future

This study revisits this particular regulation and explores new considerations regarding the molecular and cellular mechanisms of direct G protein inhibition of voltage-gated calcium channels.

Phosphorylation of the Cav3.2 T-type calcium channel directly regulates its gating properties

It is shown for the first time, to the knowledge, that Cav3.2 channels are highly phosphorylated in the mammalian brain and phosphorylation is established as an important mechanism involved in the dynamic regulation of Cav 3.2 channel gating properties.

Auxiliary subunits: essential components of the voltage-gated calcium channel complex

Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond

The aim of this Review is to examine both the classic and novel roles for these auxiliary subunits in voltage-gated calcium channel function and beyond.

Voltage-gated calcium channels.

  • W. Catterall
  • Biology
    Cold Spring Harbor perspectives in biology
  • 2011
The molecular relationships and physiological functions of these voltage-gated Ca(2+) channel proteins are presented and information on their molecular, genetic, physiological, and pharmacological properties is provided.