ArticleMolecular biology of the cell1999
Functional and biochemical analysis of the C2 domains of synaptotagmin IV.
Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 56 citations in OpenAlex.
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- Conserved expression of the zebrafishHeliyon · 2024Article
- Neuronal Scaffold Protein ARMS Interacts with Synaptotagmin-4 C2AB through the Ankyrin Repeat Domain with an Unexpected Mode.International journal of molecular sciences · 2023Article
- Gene expression profiles reveal key genes for early diagnosis and treatment of adamantinomatous craniopharyngioma.Cancer gene therapy · 2018Article
- Changes of lysosomal membrane permeabilization and lipid metabolism in sidt2 deficient mice.Experimental and therapeutic medicine · 2018Article
- Synaptotagmin 4 Regulates Pancreatic β Cell Maturation by Modulating the CaDevelopmental cell · 2018Article
- Lysosomal integral membrane protein Sidt2 plays a vital role in insulin secretion.International journal of clinical and experimental pathology · 2015Article
- Synaptotagmin IV acts as a multi-functional regulator of Ca2+-dependent exocytosis.Neurochemical research · 2011Review
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- Upregulation of synaptotagmin IV inhibits transmitter release in PC12 cells with targeted synaptotagmin I knockdown.BMC neuroscience · 2010Article
- Synaptotagmin IV determines the linear Ca2+ dependence of vesicle fusion at auditory ribbon synapses.Nature neuroscience · 2010Article
- Synaptotagmin IV: a multifunctional regulator of peptidergic nerve terminals.Nature neuroscience · 2009Article
- JNK phosphorylates synaptotagmin-4 and enhances Ca2+-evoked release.The EMBO journal · 2008Article
- Synaptotagmin IV regulates glial glutamate release.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- RNA interference-mediated silencing of synaptotagmin IX, but not synaptotagmin I, inhibits dense-core vesicle exocytosis in PC12 cells.The Biochemical journal · 2004Article
- Alternative splicing isoforms of synaptotagmin VII in the mouse, rat and human.The Biochemical journal · 2002Article
- Biogenesis of regulated exocytotic carriers in neuroendocrine cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000Article
- Deficits in memory and motor performance in synaptotagmin IV mutant mice.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Searching for depolarization-induced genes that modulate synaptic plasticity and neurotrophin-induced genes that mediate neuronal differentiation.Neurochemical research · 2000Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptotagmins (Syts) are a family of vesicle proteins that have been implicated in both regulated neurosecretion and general membrane trafficking. Calcium-dependent interactions mediated through their C2 domains are proposed to contribute to the mechanism by which Syts trigger calcium-dependent neurotransmitter release. Syt IV is a novel member of the Syt family that is induced by cell depolarization and has a rapid rate of synthesis and a short half-life. Moreover, the C2A domain of Syt IV does not bind calcium. We have examined the biochemical and functional properties of the C2 domains of Syt IV. Consistent with its non-calcium binding properties, the C2A domain of Syt IV binds syntaxin isoforms in a calcium-independent manner. In neuroendocrine pheochromocytoma (PC12) cells, Syt IV colocalizes with Syt I in the tips of the neurites. Microinjection of the C2A domain reveals that calcium-independent interactions mediated through this domain of Syt IV inhibit calcium-mediated neurotransmitter release from PC12 cells. Conversely, the C2B domain of Syt IV contains calcium binding properties, which permit homo-oligomerization as well as hetero-oligomerization with Syt I. Our observation that different combinatorial interactions exist between Syt and syntaxin isoforms, coupled with the calcium stimulated hetero-oligomerization of Syt isoforms, suggests that the secretory machinery contains a vast repertoire of biochemical properties for sensing calcium and regulating neurotransmitter release accordingly.
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