ArticleThe Journal of biological chemistry2014
The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization.The Journal of cell biology · 2024Article
- Membranes get in shape: Biophysics of curving bilayers.Biophysical journal · 2024Article
- Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Synaptotagmin 1 oligomerization via the juxtamembrane linker regulates spontaneous and evoked neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Phosphatidylinositol 4,5 Bisphosphate Controls the cis and trans Interactions of Synaptotagmin 1.Biophysical journal · 2019Article
- The juxtamembrane linker in neutral sphingomyelinase-2 functions as an intramolecular allosteric switch that activates the enzyme.The Journal of biological chemistry · 2019Article
- Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.Scientific reports · 2018Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- Choice of reconstitution protocol modulates the aggregation state of full-length membrane-reconstituted synaptotagmin-1.Protein science : a publication of the Protein Society · 2018Article
- Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR.Biophysical journal · 2018Article
- Non-Native Metal Ion Reveals the Role of Electrostatics in Synaptotagmin 1-Membrane Interactions.Biochemistry · 2017Article
- Planar Supported Membranes with Mobile SNARE Proteins and Quantitative Fluorescence Microscopy Assays to Study Synaptic Vesicle Fusion.Frontiers in molecular neuroscience · 2017Review
- Article
- Phosphorylation of synaptotagmin-1 controls a post-priming step in PKC-dependent presynaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Transmembrane tethering of synaptotagmin to synaptic vesicles controls multiple modes of neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The destructive effect of botulinum neurotoxins on the SNARE protein: SNAP-25 and synaptic membrane fusion.PeerJ · 2015Article
- Control of membrane gaps by synaptotagmin-Ca2+ measured with a novel membrane distance ruler.Nature communications · 2014Article
- Calcium sensitive ring-like oligomers formed by synaptotagmin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Synaptotagmin 1 (Syt1) is the calcium sensor for synchronous neurotransmitter release. The two C2 domains of Syt1, which may mediate fusion by bridging the vesicle and plasma membranes, are connected to the vesicle membrane by a 60-residue linker. Here, we use site-directed spin labeling and a novel total internal reflection fluorescence vesicle binding assay to characterize the juxtamembrane linker and to test the ability of reconstituted full-length Syt1 to interact with opposing membrane surfaces. EPR spectroscopy demonstrates that the majority of the linker interacts with the membrane interface, thereby limiting the extension of the C2A and C2B domains into the cytoplasm. Pulse dipolar EPR spectroscopy provides evidence that purified full-length Syt1 is oligomerized in the membrane, and mutagenesis indicates that a glycine zipper/GXXXG motif within the linker helps mediate oligomerization. The total internal reflection fluorescence-based vesicle binding assay demonstrates that full-length Syt1 that is reconstituted into supported lipid bilayers will capture vesicles containing negatively charged lipid in a Ca(2+)-dependent manner. Moreover, the rate of vesicle capture increases with Syt1 density, and mutations in the GXXXG motif that inhibit oligomerization of Syt1 reduce the rate of vesicle capture. This work demonstrates that modifications within the 60-residue linker modulate both the oligomerization of Syt1 and its ability to interact with opposing bilayers. In addition to controlling its activity, the oligomerization of Syt1 may play a role in organizing proteins within the active zone of membrane fusion.
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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.