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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair Souvik Naskar , Andrea Merino , Javier Espadas , Jayanti Singh , Aurelien Roux , Adai Colom , Harry H. Low Nature Structural & Molecular Biology 184 DOI: 10.1038/s41594-024-01401-8 Open Access Show Abstract ▼ Abstract: The ESCRT-III-like protein Vipp1 couples filament polymerization with membrane remodeling. It assembles planar sheets as well as 3D rings and helical polymers, all implicated in mitigating plastid-associated membrane stress. The architecture of Vipp1 planar sheets and helical polymers remains unknown, as do the geometric changes required to transition between polymeric forms. Here we show how cyanobacterial Vipp1 assembles into morphologically-related sheets and spirals on membranes in vitro. The spirals converge to form a central ring similar to those described in membrane budding. Cryo-EM structures of helical filaments reveal a close geometric relationship between Vipp1 helical and planar lattices. Moreover, the helical structures reveal how filaments twist—a process required for Vipp1, and likely other ESCRT-III filaments, to transition between planar and 3D architectures. Overall, our results provide a molecular model for Vipp1 ring biogenesis and a mechanism for Vipp1 membrane stabilization and repair, with implications for other ESCRT-III systems.	Nov 2024
Krios I-Titan Krios I at Diamond	Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily Jiwei Liu , Matteo Tassinari , Diorge P. De Souza , Souvik Naskar , Jeffrey K. Noel , Olga Bohuszewicz , Martin Buck , Tom A. Williams , Buzz Baum , Harry H. Low Cell 184, 3660 - 3673.e18 DOI: 10.1016/j.cell.2021.05.041 Diamond Proposal Number(s): [16942] Open Access Show Abstract ▼ Abstract: Membrane remodeling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, and ESCRT-III in eukaryotes. Here, using a combination of evolutionary and structural analyses, we show that these protein families are homologous and share a common ancient evolutionary origin that likely predates the last universal common ancestor. This homology is evident in cryo-electron microscopy structures of Vipp1 rings from the cyanobacterium Nostoc punctiforme presented over a range of symmetries. Each ring is assembled from rungs that stack and progressively tilt to form dome-shaped curvature. Assembly is facilitated by hinges in the Vipp1 monomer, similar to those in ESCRT-III proteins, which allow the formation of flexible polymers. Rings have an inner lumen that is able to bind and deform membranes. Collectively, these data suggest conserved mechanistic principles that underlie Vipp1, PspA, and ESCRT-III-dependent membrane remodeling across all domains of life.	Jul 2021

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