ArticlePflugers Archiv : European journal of physiology2015
The Cav1.2 N terminus contains a CaM kinase site that modulates channel trafficking and function.
Article in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- CaMKII clusters neuronal LTCCs in biomolecular condensates to gate excitation-transcription coupling.bioRxiv : the preprint server for biology · 2025Article
- Cardiac L-type calcium channel regulation by Leucine-Rich Repeat-Containing Protein 10.Channels (Austin, Tex.) · 2024Review
- Calmodulin promotes a CaFEBS letters · 2022Article
- L-Type CaBiomolecules · 2021Review
- Regulation of cardiovascular calcium channel activity by post-translational modifications or interacting proteins.Pflugers Archiv : European journal of physiology · 2020Review
- Voltage-Gated Calcium Channels: Key Players in Sensory Coding in the Retina and the Inner Ear.Physiological reviews · 2018Review
- Rapid Turnover of the Cardiac L-Type CaiScience · 2018Article
- A novel mechanism for CaThe Journal of biological chemistry · 2017Article
- Protein kinase A regulates C-terminally truncated CaThe Journal of physiology · 2017Article
- Densin-180 Controls the Trafficking and Signaling of L-Type Voltage-Gated CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Trafficking of neuronal calcium channels.Neuronal signaling · 2017Review
- The amino-terminus of high voltage activated calcium channels: CaM you or can't you?Channels (Austin, Tex.) · 2014Article
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Authors and funding
4 authors.
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Abstract
The L-type voltage-gated calcium channel Cav1.2 and the calcium-activated CaM kinase cascade both regulate excitation transcription coupling in the brain. CaM kinase is known to associate with the C terminus of Cav1.2 in a region called the PreIQ-IQ domain, which also binds multiple calmodulin molecules. Here we identify and characterize a second CaMKII binding site in the N terminus of Cav1.2 that is formed by a stretch of four amino residues (cysteine-isoleucine-serine-isoleucine) and which regulates channel expression and function. By using live cell imaging of tsA-201 cells we show that GFP fusion constructs of the CaMKII binding region, termed N2B-II co-localize with mCherry-CaMKII. Mutating CISI to AAAA ablates binding to and colocalization with CaMKII. Cav1.2-AAAA channels show reduced cell surface expression in tsA-201 cells, but interestingly, display an increase in channel function that offsets the trafficking deficit. Altogether our data reveal that the proximal N terminus of Cav1.2 contains a CaMKII binding region which contributes to channel surface expression and function.
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