ArticlePflugers Archiv : European journal of physiology2014
A novel calmodulin site in the Cav1.2 N-terminus regulates calcium-dependent inactivation.
Article in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 26 citations in OpenAlex.
- Asymmetric contribution of a selectivity filter gate in triggering inactivation of CaV1.3 channels.The Journal of general physiology · 2024Article
- Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023Review
- L-type CaPhysiological reports · 2022Article
- Calmodulin binds to the N-terminal domain of the cardiac sodium channel NaChannels (Austin, Tex.) · 2020Article
- Alternative Splicing at N Terminus and Domain I Modulates CaBiophysical journal · 2018Article
- A T-type channel-calmodulin complex triggers αCaMKII activation.Molecular brain · 2017Article
- Trafficking of neuronal calcium channels.Neuronal signaling · 2017Review
- The Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic Potential.Pharmacological reviews · 2015Review
- The Cav1.2 N terminus contains a CaM kinase site that modulates channel trafficking and function.Pflugers Archiv : European journal of physiology · 2015Article
- Comparative biochemical analysis of three members of the Schistosoma mansoni TAL family: Differences in ion and drug binding properties.Biochimie · 2015Article
- Calmodulin regulation (calmodulation) of voltage-gated calcium channels.The Journal of general physiology · 2014Review
- Effect of the Brugada syndrome mutation A39V on calmodulin regulation of Cav1.2 channels.Molecular brain · 2014Article
- Article
- The amino-terminus of high voltage activated calcium channels: CaM you or can't you?Channels (Austin, Tex.) · 2014Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The L-type voltage-gated calcium channel Cav1.2 is important for excitation-contraction coupling in the heart, as well as CREB-mediated transcription in the brain. The ubiquitous calcium-binding protein calmodulin (CaM) is known to modulate calcium-dependent inactivation (CDI) of these channels, thus limiting the amount of calcium entering via Cav1.2 during prolonged or repetitive membrane depolarizations. The proximal N-terminus of Cav1.2 contains a CaM-binding site at residue W52 that is critical for a type of CDI that is mediated by the N-terminal lobe of CaM. Here, we identify a second CaM interaction site in the Cav1.2 N-terminus downstream of the W52 site that is formed by residue C106. We show by site-directed mutagenesis coupled with electrophysiological measurements that this region of the channel functionally partakes in N-lobe CDI, likely by acting as a gating transduction motif. Thus, our data indicate that calcium regulation of Cav1.2 channels is more complex than previously thought, and involves more than one region within the channel's N-terminal domain.
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