Informace o publikaci
Membrane remodeling and higher-order structure formation by DivIVA
| Autoři | |
|---|---|
| Rok publikování | 2026 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | International journal of biological macromolecules |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | https://www.sciencedirect.com/science/article/pii/S0141813026013140?pes=vor&utm_source=clarivate&getft_integrator=clarivate |
| Doi | https://doi.org/10.1016/j.ijbiomac.2026.151388 |
| Klíčová slova | Cell division; Membrane remodeling; Membrane fusion; DivIVA; Min system; SNARE complex; BAR proteins |
| Popis | Membrane dynamics, including remodeling, fusion and fission, are essential in both prokaryotic and eukaryotic cells. They are involved in processes such as cell division, intracellular transport, and the maintenance of organelle structure. In eukaryotes, these processes are regulated by complex systems, such as the SNARE complex and dynamin-related proteins. Prokaryotes, which possess a simpler cellular organization, employ flotillins and dynamin-like proteins for membrane modulation and rely on cytoskeletal components and Min proteins to control cell division septum positioning. Cardiolipin, a phospholipid enriched at sites of membrane curvature, participates in modulating membrane morphology. In gram-positive bacteria, the peripheral membrane protein DivIVA exhibits higher affinity for cardiolipin and localizes to sites of negative curvature. DivIVA is a topological determinant of many proteins, including the Min proteins, which negatively regulate cell division. Although DivIVA helps control the spatial positioning of cell division, the mechanisms of its membrane interaction and influence on morphology remain unclear. Here, we show that DivIVA forms higher-order assemblies on the membrane and enhances changes in membrane morphology. These findings support the hypothesis that DivIVA might have an active role in membrane remodeling and provide insights into the interaction between this bacterial protein and the membrane. |
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