Annexins induce curvature on free-edge membranes displaying distinct morphologies
| Autor: | Kenji Maeda, Jesper Nylandsted, Weria Pezeshkian, Vita Solovyeva, Jonas Camillus Jeppesen, Adam Cohen Simonsen, Theresa Louise Boye |
|---|---|
| Přispěvatelé: | Molecular Dynamics |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Models Molecular Protein family Annexins CALCIUM-DEPENDENT BINDING Lipid Bilayers lcsh:Medicine PROTEIN Curvature Microscopy Atomic Force Article 03 medical and health sciences FUSION Annexin SYNEXIN Humans CORE Lipid bilayer lcsh:Science LIPID-BILAYERS chemistry.chemical_classification N-TERMINAL DOMAIN Multidisciplinary Chemistry lcsh:R AGGREGATION Recombinant Proteins Amino acid SELF-ASSOCIATION Folding (chemistry) 030104 developmental biology Membrane Microscopy Fluorescence Membrane curvature Biophysics lcsh:Q Aluminum Silicates MOLECULAR-STRUCTURE |
| Zdroj: | Boye, T L, Jeppesen, J C, Maeda, K, Pezeshkian, W, Solovyeva, V, Nylandsted, J & Simonsen, A C 2018, ' Annexins induce curvature on free-edge membranes displaying distinct morphologies ', Scientific Reports, vol. 8, no. 1, 10309 . https://doi.org/10.1038/s41598-018-28481-z Scientific Reports Scientific Reports, Vol 8, Iss 1, Pp 1-14 (2018) Boye, T L, Jeppesen, J C, Maeda, K, Pezeshkian, W, Solovyeva, V, Nylandsted, J & Simonsen, A C 2018, ' Annexins induce curvature on free-edge membranes displaying distinct morphologies ', Scientific Reports, vol. 8, 10309 . https://doi.org/10.1038/s41598-018-28481-z Scientific Reports, 8:10309. Nature Publishing Group |
| ISSN: | 2045-2322 |
| Popis: | Annexins are a family of proteins characterized by their ability to bind anionic membranes in response to Ca2+-activation. They are involved in a multitude of cellular functions including vesiculation and membrane repair. Here, we investigate the effect of nine annexins (ANXA1-ANXA7, ANXA11, ANXA13) on negatively charged double supported membrane patches with free edges. We find that annexin members can be classified according to the membrane morphology they induce and matching a dendrogam of the annexin family based on full amino acid sequences. ANXA1 and ANXA2 induce membrane folding and blebbing initiated from membrane structural defects inside patches while ANXA6 induces membrane folding originating both from defects and from the membrane edges. ANXA4 and ANXA5 induce cooperative roll-up of the membrane starting from free edges, producing large rolls. In contrast, ANXA3 and ANXA13 roll the membrane in a fragmented manner producing multiple thin rolls. In addition to rolling, ANXA7 and ANXA11 are characterized by their ability to form fluid lenses localized between the membrane leaflets. A shared feature necessary for generating these morphologies is the ability to induce membrane curvature on free edged anionic membranes. Consequently, induction of membrane curvature may be a significant property of the annexin protein family that is important for their function. |
| Databáze: | OpenAIRE |
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