Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms
| العنوان: | Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms |
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| المؤلفون: | Raya Sorkin, Rashmi Voleti, Josep Rizo, Guy Brand, Emma Logtenberg, Melissa C. Piontek, Gijs J.L. Wuite, Wouter H. Roos, Margherita Marchetti, Alexander J. Groffen, Emma Kerklingh |
| المساهمون: | Physics of Living Systems, LaserLaB - Molecular Biophysics, Functional Genomics, Molecular Biophysics, Human genetics, Amsterdam Neuroscience - Cellular & Molecular Mechanisms |
| المصدر: | Sorkin, R, Marchetti, M, Logtenberg, E, Piontek, M C, Kerklingh, E, Brand, G, Voleti, R, Rizo, J, Roos, W H, Groffen, A J & Wuite, G J L 2020, ' Synaptotagmin-1 and Doc2b Exhibit Distinct Membrane-Remodeling Mechanisms ', Biophysical Journal, vol. 118, no. 3, pp. 643-656 . https://doi.org/10.1016/j.bpj.2019.12.021 Biophysical Journal, 118(3), 643-656. Biophysical Society Biophysical Journal, 118(3), 643-656. CELL PRESS Biophys J |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Biophysics, chemistry.chemical_element, Nerve Tissue Proteins, Calcium, Neurotransmission, SYT1, Membrane Fusion, Synaptic Transmission, Synaptotagmin 1, 03 medical and health sciences, 0302 clinical medicine, Humans, SDG 7 - Affordable and Clean Energy, 030304 developmental biology, 0303 health sciences, Fusion, Chemistry, Tethering, Calcium-Binding Proteins, Articles, DOC2B, Membrane, Synaptotagmin I, SNARE Proteins, 030217 neurology & neurosurgery, Protein Binding |
| الوصف: | Synaptotagmin-1 (Syt1) is a calcium sensor protein that is critical for neurotransmission and is therefore extensively studied. Here, we use pairs of optically trapped beads coated with SNARE-free synthetic membranes to investigate Syt1-induced membrane remodeling. This activity is compared with that of Doc2b, which contains a conserved C2AB domain and induces membrane tethering and hemifusion in this cell-free model. We find that the soluble C2AB domain of Syt1 strongly affects the probability and strength of membrane-membrane interactions in a strictly Ca2+- and protein-dependent manner. Single-membrane loading of Syt1 yielded the highest probability and force of membrane interactions, whereas in contrast, Doc2b was more effective after loading both membranes. A lipid-mixing assay with confocal imaging reveals that both Syt1 and Doc2b are able to induce hemifusion; however, significantly higher Syt1 concentrations are required. Consistently, both C2AB fragments cause a reduction in the membrane-bending modulus, as measured by a method based on atomic force microscopy. This lowering of the energy required for membrane deformation may contribute to Ca2+-induced fusion. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0006-3495 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b9f406d103fb959991bea979af8e0a6 https://doi.org/10.1016/j.bpj.2019.12.021 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....8b9f406d103fb959991bea979af8e0a6 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00063495 |
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