The accessory α2δ subunits of voltage-gated calcium channels are type 1 transmembrane proteins that are highly glycosylated and possess multiple disulfide bonds. From studies of the topology and processing of skeletal-muscle α2δ-1, it has been shown to be post-translationally cleaved into an α2 and a δ subunit, which remain disulfide-bonded. In the present study, we have examined the processing of α2δ-2 subunits when stably or transiently expressed, in tsA (temperature-sensitive A)-201, Cos-7 and NG108-15 cells, and compared it with that observed in the cerebellum. Despite showing full functionality and being expressed on the plasma membrane, the vast majority of heterologously expressed α2δ-2 is not cleaved into α2-2 and δ-2, unlike endogenous α2δ-2 in the cerebellum. It remains an open question for future research whether α2δ-2 is functional in its calcium channel trafficking role in its proteolytically cleaved or non-cleaved state.
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Conference Article|
October 25 2006
Do voltage-gated calcium channel α2δ subunits require proteolytic processing into α2 and δ to be functional?
L. Douglas;
L. Douglas
1Department of Pharmacology, University College London, London WC1E 6BT, U.K.
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A. Davies;
A. Davies
1Department of Pharmacology, University College London, London WC1E 6BT, U.K.
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J. Wratten;
J. Wratten
1Department of Pharmacology, University College London, London WC1E 6BT, U.K.
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A.C. Dolphin
A.C. Dolphin
1
1Department of Pharmacology, University College London, London WC1E 6BT, U.K.
1To whom correspondence should be addressed, at Laboratory of Cellular and Molecular Neuroscience, Department of Pharmacology, University College London (email a.dolphin@ucl.ac.uk).
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Publisher: Portland Press Ltd
Received:
July 20 2006
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (5): 894–898.
Article history
Received:
July 20 2006
Citation
L. Douglas, A. Davies, J. Wratten, A.C. Dolphin; Do voltage-gated calcium channel α2δ subunits require proteolytic processing into α2 and δ to be functional?. Biochem Soc Trans 1 October 2006; 34 (5): 894–898. doi: https://doi.org/10.1042/BST0340894
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