%0 Journal Article
%A Junglas, Benedikt
%A Kartte, David
%A Kutzner, Mirka
%A Hellmann, Nadja
%A Ritter, Ilona
%A Schneider, Dirk
%A Sachse, Carsten
%T Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies
%J Nature structural & molecular biology
%V 32
%@ 1545-9993
%C London [u.a.]
%I Nature Publishing Group
%M FZJ-2024-05814
%P 555–570
%D 2025
%X Vesicle-inducing protein in plastids 1 (Vipp1) is critical for thylakoid membrane biogenesis and maintenance. Although Vipp1 has recently been identified as a member of the endosomal sorting complexes required for transport III superfamily, it is still unknown how Vipp1 remodels membranes. Here, we present cryo-electron microscopy structures of Synechocystis Vipp1 interacting with membranes: seven structures of helical and stacked-ring assemblies at 5-7-Å resolution engulfing membranes and three carpet structures covering lipid vesicles at ~20-Å resolution using subtomogram averaging. By analyzing ten structures of N-terminally truncated Vipp1, we show that helix α0 is essential for membrane tubulation and forms the membrane-anchoring domain of Vipp1. Lastly, using a conformation-restrained Vipp1 mutant, we reduced the structural plasticity of Vipp1 and determined two structures of Vipp1 at 3.0-Å resolution, resolving the molecular details of membrane-anchoring and intersubunit contacts of helix α0. Our data reveal membrane curvature-dependent structural transitions from carpets to rings and rods, some of which are capable of inducing and/or stabilizing high local membrane curvature triggering membrane fusion.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 39379528
%U <Go to ISI:>//WOS:001331270100001
%R 10.1038/s41594-024-01399-z
%U https://juser.fz-juelich.de/record/1031787