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.
Do voltage-gated calcium channel α2δ subunits require proteolytic processing into α2 and δ to be functional?
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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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