ArticleProceedings of the National Academy of Sciences of the United States of America2004
Deletion of the synaptic protein interaction site of the N-type (CaV2.2) calcium channel inhibits secretion in mouse pheochromocytoma cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
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- CAV2 promotes the growth of renal cell carcinoma through the EGFR/PI3K/Akt pathway.OncoTargets and therapy · 2018Article
- Cross talk between β subunits, intracellular CaPhysiological reports · 2018Article
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- Regulation of insulin exocytosis by calcium-dependent protein kinase C in beta cells.Cell calcium · 2017Review
- Regulation of Ca2+ channels by SNAP-25 via recruitment of syntaxin-1 from plasma membrane clusters.Molecular biology of the cell · 2016Article
- Article
- How do T-type calcium channels control low-threshold exocytosis?Communicative & integrative biology · 2012Article
- A Ca(v)3.2/syntaxin-1A signaling complex controls T-type channel activity and low-threshold exocytosis.The Journal of biological chemistry · 2012Article
- A mutation in the first intracellular loop of CACNA1A prevents P/Q channel modulation by SNARE proteins and lowers exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Involvement of Ca2+ channel synprint site in synaptic vesicle endocytosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Selective disruption of the mammalian secretory apparatus enhances or eliminates calcium current modulation in nerve endings.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Adaptive depression in synaptic transmission in the nucleus of the solitary tract after in vivo chronic intermittent hypoxia: evidence for homeostatic plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- K+ channel facilitation of exocytosis by dynamic interaction with syntaxin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Psychostimulants, madness, memory... and RGS proteins?Neuromolecular medicine · 2005Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Presynaptic N-type Ca2+ channels (CaV2.2, alpha1B) are thought to bind to SNARE (SNAP-25 receptor) complex proteins through a synaptic protein interaction (synprint) site on the intracellular loop between domains II and III of the alpha1B subunit. Whether binding of syntaxin to the N-type Ca2+ channels is required for coupling Ca2+ ion influx to rapid exocytosis has been the subject of considerable investigation. In this study, we deleted the synprint site from a recombinant alpha1B Ca2+ channel subunit and transiently transfected either the wild-type alpha1B or the synprint deletion mutant into mouse pheochromocytoma (MPC) cell line 9/3L, a cell line that has the machinery required for rapid stimulated exocytosis but lacks endogenous voltage-dependent Ca2+ channels. Secretion was elicited by activation of exogenously transfected Ca2+ channel subunits. The current-voltage relationship was similar for the wild-type and mutant alpha1B-containing Ca2+ channels. Although total Ca2+ entry was slightly larger for the synprint deletion channel, compared with the wild-type channel, when Ca2+ entry was normalized to cell size and limited to cells with similar Ca2+ entry (approximately 150 x 10(6) Ca2+ ions/pF cell size), total secretion and the rate of secretion, determined by capacitance measurements, were significantly reduced in cells expressing the synprint deletion mutant channels, compared with wild-type channels. Furthermore, the amount of endocytosis was significantly reduced in cells with the alpha1B synprint deletion mutant, compared with the wild-type subunit. These results suggest that the synprint site is necessary for efficient coupling of Ca2+ influx through alpha1B-containing Ca2+ channels to exocytosis.
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