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Review
. 2008 Apr 15;586(8):2035-7.
doi: 10.1113/jphysiol.2008.152298. Epub 2008 Feb 21.

Does the voltage-gated calcium channel alpha2delta-1 subunit play a dual function in skeletal muscle?

Norbert Weiss  1 , Ekaterina Ivanova
Affiliations
Review

Does the voltage-gated calcium channel alpha2delta-1 subunit play a dual function in skeletal muscle?

Norbert Weiss et al. J Physiol. .
No abstract available

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Figures

Figure 1
Figure 1. Structural organization of the voltage-gated Ca2+ channel α2δ-1 subunit and its potential functions in the skeletal muscle
In skeletal muscle, the dihydropyridine receptor (DHPR) is composed of the Cav1.1 subunit (blue), surrounded by auxiliary β1a (red), γ (orange) and α2δ-1 (green) subunits. The α2δ-1 subunit is the product of a unique gene, post-translationally cleaved into α2 and δ peptides remaining associated by disulphide bonds (S–S), and highly glycosylated. On the basis of hydrophobicity studies and direct-site mutagenesis, it was proposed that the α2 subunit is completely extracellular, while a unique transmembrane helix formed by the carboxy-terminale region of the δ subunit allows the anchoring of α2δ-1 at the plasma membrane. Sequence analysis revealed the presence of a von Willebrand factor type A (VWA) domain, habitually involved in divalent-cation-dependent interactions with the extracellular matrix. Two Cache domains have also been identified and could be relevant for gabapentinoid drugs binding to the α2δ-1 subunit.
See this image and copyright information in PMC

Comment on

References

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