AKAP79 modulation of L-type channels involves disruption of intramolecular interactions in the CaV1.2 subunit

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dc.contributor.authorAltier, Christophe
dc.contributor.authorDubel, Stefan J.
dc.contributor.authorBarrère, Christian
dc.contributor.authorJarvis, Scott E.
dc.contributor.authorStotz, Stephanie C.
dc.contributor.authorScott, John D.
dc.contributor.authorNargeot, Joël
dc.contributor.authorZamponi, Gerald W.
dc.contributor.authorBourinet, Emmanuel
dc.date.accessioned2018-05-29T19:31:59Z
dc.date.available2018-05-29T19:31:59Z
dc.date.issued2012-05
dc.description.abstractL-type voltage gated calcium channels (VGCCs) interact with a variety of proteins that modulate both their function and localization. A-Kinase Anchoring Proteins (AKAPs) facilitate L-type calcium channel phosphorylation through β adrenergic stimulation. Our previous work indicated a role of neuronal AKAP79/150 in the membrane targeting of Ca(V)1.2 L-type calcium channels, which involved a proline rich domain (PRD) in the intracellular II-III loop of the channel.(1) Here, we show that mutation of proline 857 to alanine (P857A) into the PRD does not disrupt the AKAP79-induced increase in Ca(v)1.2 membrane expression. Furthermore, deletion of two other PRDs into the carboxy terminal domain of Ca(V)1.2 did not alter the targeting role of AKAP79. In contrast, the distal carboxy terminus region of the channel directly interacts with AKAP79. This protein-protein interaction competes with a direct association of the channel II-III linker on the carboxy terminal tail and modulates membrane targeting of Ca(V)1.2. Thus, our results suggest that the effects of AKAP79 occur through relief of an autoinhibitory mechanism mediated by intramolecular interactions of Ca(v)1.2 intracellular regions.en_US
dc.identifier.citationAltier, C., Dubel, S. J., Barrere, C., Jarvis, S. E., Stotz, S. C., Scott, J. D., … Bourinet, E. (2012). AKAP79 modulation of L-type channels involves disruption of intramolecular interactions in the Cav1.2 subunit. Channels. Taylor and Francis Inc. https://doi.org/10.4161/chan.20865en_US
dc.identifier.doihttp://dx.doi.org/10.4161/chan.20865en_US
dc.identifier.urihttp://hdl.handle.net/1880/106706
dc.identifier.urihttps://doi.org/10.11575/PRISM/43737
dc.language.isoenen_US
dc.publisherLandes Bioscienceen_US
dc.publisher.departmentPhysiology & Pharmacologyen_US
dc.publisher.facultyCumming School of Medicineen_US
dc.publisher.institutionUniversity of Calgaryen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.titleAKAP79 modulation of L-type channels involves disruption of intramolecular interactions in the CaV1.2 subuniten_US
dc.typejournal articleen_US
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