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Circular oligomerization is an intrinsic property of synaptotagmin
- Source :
- eLife, eLife, eLife Sciences Publication, 2017, 6, pp.e27441. ⟨10.7554/eLife.27441⟩, eLife, 2017, 6, pp.e27441. ⟨10.7554/eLife.27441⟩, eLife, Vol 6 (2017)
- Publication Year :
- 2017
- Publisher :
- HAL CCSD, 2017.
-
Abstract
- Previously, we showed that synaptotagmin1 (Syt1) forms Ca2+-sensitive ring-like oligomers on membranes containing acidic lipids and proposed a potential role in regulating neurotransmitter release (Zanetti et al., 2016). Here, we report that Syt1 assembles into similar ring-like oligomers in solution when triggered by naturally occurring polyphosphates (PIP2 and ATP) and magnesium ions (Mg2+). These soluble Syt1 rings were observed by electron microscopy and independently demonstrated and quantified using fluorescence correlation spectroscopy. Oligomerization is triggered when polyphosphates bind to the polylysine patch in C2B domain and is stabilized by Mg2+, which neutralizes the Ca2+-binding aspartic acids that likely contribute to the C2B interface in the oligomer. Overall, our data show that ring-like polymerization is an intrinsic property of Syt1 with reasonable affinity that can be triggered by the vesicle docking C2B-PIP2 interaction and raise the possibility that Syt1 rings could pre-form on the synaptic vesicle to facilitate docking.
- Subjects :
- Phosphatidylinositol 4,5-Diphosphate
0301 basic medicine
Cations, Divalent
QH301-705.5
Recombinant Fusion Proteins
Science
Vesicle docking
Genetic Vectors
membrane fusion
Gene Expression
Inositol 1,4,5-Trisphosphate
Oligomer
Synaptic vesicle
neurotransmitters
General Biochemistry, Genetics and Molecular Biology
Synaptotagmin 1
03 medical and health sciences
chemistry.chemical_compound
Adenosine Triphosphate
Escherichia coli
Magnesium
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Amino Acid Sequence
Cloning, Molecular
Biology (General)
Magnesium ion
electron microscopy
General Immunology and Microbiology
General Neuroscience
Synaptotagmin I
E. coli
General Medicine
Cell biology
030104 developmental biology
Membrane
chemistry
Polylysine
Biophysics
Medicine
Synaptic Vesicles
Protein Multimerization
Research Advance
Neuroscience
Subjects
Details
- Language :
- English
- ISSN :
- 2050084X
- Database :
- OpenAIRE
- Journal :
- eLife, eLife, eLife Sciences Publication, 2017, 6, pp.e27441. ⟨10.7554/eLife.27441⟩, eLife, 2017, 6, pp.e27441. ⟨10.7554/eLife.27441⟩, eLife, Vol 6 (2017)
- Accession number :
- edsair.doi.dedup.....c0d6c5dabf9c76965e40e18447dc953e