ArticleThe Journal of biological chemistry2009
Calmodulin is a functional regulator of Cav1.4 L-type Ca2+ channels.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Inactivation of CaV1 and CaV2 channels.The Journal of general physiology · 2025Review
- Enforced tethering elongates the cortical endoplasmic reticulum and limits store-operated Ca2+ entry.Journal of cell science · 2022Article
- Cav1.4 dysfunction and congenital stationary night blindness type 2.Pflugers Archiv : European journal of physiology · 2021Review
- Cataloguing and Selection of mRNAs Localized to Dendrites in Neurons and Regulated by RNA-Binding Proteins in RNA Granules.Biomolecules · 2020Review
- Splicing of an automodulatory domain in CaThe Journal of general physiology · 2018Article
- Channeling Vision: CaBioMed research international · 2018Review
- Characterization of C-terminal Splice Variants of Cav1.4 Ca2+ Channels in Human Retina.The Journal of biological chemistry · 2016Article
- A rendezvous with the queen of ion channels: Three decades of ion channel research by David T Yue and his Calcium Signals Laboratory.Channels (Austin, Tex.) · 2016Article
- Towards a Unified Theory of Calmodulin Regulation (Calmodulation) of Voltage-Gated Calcium and Sodium Channels.Current molecular pharmacology · 2015Review
- Voltage-Gated Cav1 Channels in Disorders of Vision and Hearing.Current molecular pharmacology · 2015Review
- Calmodulin enhances ribbon replenishment and shapes filtering of synaptic transmission by cone photoreceptors.The Journal of general physiology · 2014Article
- The amino-terminus of high voltage activated calcium channels: CaM you or can't you?Channels (Austin, Tex.) · 2014Article
- Alterations of sodium and potassium channels of RGCs in RCS rat with the development of retinal degeneration.Journal of molecular neuroscience : MN · 2013Article
- Oligomerization and Ca2+/calmodulin control binding of the ER Ca2+-sensors STIM1 and STIM2 to plasma membrane lipids.Bioscience reports · 2013Article
- Complex regulation of voltage-dependent activation and inactivation properties of retinal voltage-gated Cav1.4 L-type Ca2+ channels by Ca2+-binding protein 4 (CaBP4).The Journal of biological chemistry · 2012Article
- Trafficking and stability of voltage-gated calcium channels.Cellular and molecular life sciences : CMLS · 2012Review
- Alternative splicing at C terminus of Ca(V)1.4 calcium channel modulates calcium-dependent inactivation, activation potential, and current density.The Journal of biological chemistry · 2012Article
- The dynamic architecture of photoreceptor ribbon synapses: cytoskeletal, extracellular matrix, and intramembrane proteins.Visual neuroscience · 2011Review
- The glutamic acid-rich protein is a gating inhibitor of cyclic nucleotide-gated channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Channelopathies in Cav1.1, Cav1.3, and Cav1.4 voltage-gated L-type Ca2+ channels.Pflugers Archiv : European journal of physiology · 2010Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cav1.4 channels are unique among the high voltage-activated Ca2+ channel family because they completely lack Ca2+-dependent inactivation and display very slow voltage-dependent inactivation. Both properties are of crucial importance in ribbon synapses of retinal photoreceptors and bipolar cells, where sustained Ca2+ influx through Cav1.4 channels is required to couple slow graded changes of the membrane potential with tonic glutamate release. Loss of Cav1.4 function causes severe impairment of retinal circuitry function and has been linked to night blindness in humans and mice. Recently, an inhibitory domain (ICDI: inhibitor of Ca2+-dependent inactivation) in the C-terminal tail of Cav1.4 has been discovered that eliminates Ca2+-dependent inactivation by binding to upstream regulatory motifs within the proximal C terminus. The mechanism underlying the action of ICDI is unclear. It was proposed that ICDI competitively displaces the Ca2+ sensor calmodulin. Alternatively, the ICDI domain and calmodulin may bind to different portions of the C terminus and act independently of each other. In the present study, we used fluorescence resonance energy transfer experiments with genetically engineered cyan fluorescent protein variants to address this issue. Our data indicate that calmodulin is preassociated with the C terminus of Cav1.4 but may be tethered in a different steric orientation as compared with other Ca2+ channels. We also find that calmodulin is important for Cav1.4 function because it increases current density and slows down voltage-dependent inactivation. Our data show that the ICDI domain selectively abolishes Ca2+-dependent inactivation, whereas it does not interfere with other calmodulin effects.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.