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Membrane binding and subcellular targeting of C2 domains
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006C2 domains are a ubiquitous structural module and many of them function in Ca2+ -dependent membrane binding and thereby serve as Ca2+ effectors for divergent Ca2+ -mediated cellular processes. Extensive structural, biochemical, biophysical, and cellular studies of C2 domains and host proteins in the past decade have shown that due to their structural ...
Wonhwa, Cho, Robert V, Stahelin
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Science Signaling, 2001
The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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Crystal structure of human Intersectin-2L C2 domain
Biochemical and Biophysical Research Communications, 2013Intersectin-2L (ITSN-2L) is a long isoform of ITSN family, which is a multimodule scaffolding protein functioning in membrane-associated molecular trafficking and signal transduction pathways. ITSN-2L possesses a carboxy-terminal extension encoding a Dbl homology domain (DH), a pleckstrin homology domain (PH) and a C2 domain, suggesting that it could ...
Wei, Zhang +7 more
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Trends in Neurosciences, 2003
Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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The C2 domains of synaptotagmin – partners in exocytosis
Trends in Biochemical Sciences, 2004Rapid signaling between neurons relies on the Ca(2+)-triggered exocytosis of neurotransmitters. Release is mediated by 'kiss-and-run' or complete fusion of secretory organelles with the plasma membrane. Current models indicate that exocytosis is regulated by synaptotagmin I (syt) and mediated by SNARE (soluble NSF-attachment protein receptor) proteins.
Jihong, Bai, Edwin R, Chapman
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The Role of C2 Domains in PKC Signaling
2012More than two decades ago, the discovery of the first C2 domain in conventional Protein Kinase Cs (cPKCs) and of its role as a calcium-binding motif began to shed light on the activation mechanism of this family of Serine/Threonine kinases which are involved in several critical signal transduction pathways.
Carole A, Farah, Wayne S, Sossin
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C2 domain conformational changes in phospholipase C-δ1
Nature Structural & Molecular Biology, 1996The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical.
J A, Grobler +3 more
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Otoferlin: a multi-C2 domain protein essential for hearing
Trends in Neurosciences, 2012Sound is encoded at synapses between cochlear inner hair cells and the auditory nerve. These synapses are anatomically and functionally specialized to transmit acoustic information with high fidelity over a lifetime. The molecular mechanisms of hair-cell transmitter release have recently attracted substantial interest.
Tina, Pangršič +2 more
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Arabidopsis PLDs with C2‐domain function distinctively in hypoxia
Physiologia Plantarum, 2018Hypoxia (oxygen deprivation) causes metabolic disturbances at physiological, biochemical and genetic levels and results in decreased plant growth and development. Phospholipase D (PLD)‐mediated signaling was reported for abiotic and biotic stress signaling events in plants.
Premkumar, Albert +4 more
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Analysis of Protein–Lipid Interactions Using Purified C2 Domains
2016C2 domains (C2s) are regulatory protein modules identified in eukaryotic proteins targeted to cell membranes. C2s were initially characterized as independently folded Ca(2+)-dependent phospholipids binding domains; however, later studies have shown that C2s have evolutionarily diverged into Ca(2+)-dependent and Ca(2+)-independent forms.
Perez-Sancho, Jessica +3 more
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