ArticleBiochemistry2011
Phosphatidylinositol 4,5-bisphosphate alters synaptotagmin 1 membrane docking and drives opposing bilayers closer together.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 61 citations in OpenAlex.
- PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025Review
- A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.bioRxiv : the preprint server for biology · 2024Article
- A lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.bioRxiv : the preprint server for biology · 2024Article
- Review
- On the difficulties of characterizing weak protein interactions that are critical for neurotransmitter release.FEBS open bio · 2022Review
- Polybasic Patches in Both C2 Domains of Synaptotagmin-1 Are Required for Evoked Neurotransmitter Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Synaptotagmin-1 C2B domains cooperatively stabilize the fusion stalkChemical science · 2022Article
- Article
- The neuronal calcium sensor Synaptotagmin-1 and SNARE proteins cooperate to dilate fusion pores.eLife · 2021Article
- SNARE complex alters the interactions of the CaBiophysical journal · 2021Article
- Synaptotagmin-1 membrane binding is driven by the C2B domain and assisted cooperatively by the C2A domain.Scientific reports · 2020Article
- Membrane Association and Functional Mechanism of Synaptotagmin-1 in Triggering Vesicle Fusion.Biophysical journal · 2020Article
- Partial Metal Ion Saturation of C2 Domains Primes Synaptotagmin 1-Membrane Interactions.Biophysical journal · 2020Article
- Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms.Biophysical journal · 2020Article
- Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.Progress in nuclear magnetic resonance spectroscopy · 2018Review
- Non-Native Metal Ion Reveals the Role of Electrostatics in Synaptotagmin 1-Membrane Interactions.Biochemistry · 2017Article
- PtdInsPeLife · 2016Article
- PI(4,5)P₂-binding effector proteins for vesicle exocytosis.Biochimica et biophysica acta · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Synaptotagmin 1 (syt1) is a synaptic vesicle-anchored membrane protein that acts as the calcium sensor for the synchronous component of neuronal exocytosis. Using site-directed spin labeling, the position and membrane interactions of a fragment of syt1 containing its two C2 domains (syt1C2AB) were assessed in bilayers containing phosphatidylcholine (PC), phosphatidylserine (PS), and phosphatidylinositol 4,5-bisphosphate (PIP(2)). Addition of 1 mol % PIP(2) to a lipid mixture of PC and PS results in a deeper membrane penetration of the C2A domain and alters the orientation of the C2B domain so that the polybasic face of C2B comes into the proximity of the bilayer interface. The C2B domain is found to contact the membrane interface in two regions, the Ca(2+)-binding loops and a region opposite the Ca(2+)-binding loops. This suggests that syt1C2AB is configured to bridge two bilayers and is consistent with a model generated previously for syt1C2AB bound to membranes of PC and PS. Point-to-plane depth restraints, obtained by progressive power saturation, and interdomain distance restraints, obtained by double electron-electron resonance, were obtained in the presence of PIP(2) and used in a simulated annealing routine to dock syt1C2AB to two membrane interfaces. The results yield an average structure different from what is found in the absence of PIP(2) and indicate that bilayer-bilayer spacing is decreased in the presence of PIP(2). The results indicate that PIP(2), which is necessary for bilayer fusion, alters C2 domain orientation, enhances syt1-membrane electrostatic interactions, and acts to drive vesicle and cytoplasmic membrane surfaces closer together.
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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.