TY  - JOUR
AU  - Junglas, Benedikt
AU  - Kartte, David
AU  - Kutzner, Mirka
AU  - Hellmann, Nadja
AU  - Ritter, Ilona
AU  - Schneider, Dirk
AU  - Sachse, Carsten
TI  - Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies
JO  - Nature structural & molecular biology
VL  - 32
SN  - 1545-9993
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - FZJ-2024-05814
SP  - 555–570
PY  - 2025
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 39379528
UR  - <Go to ISI:>//WOS:001331270100001
DO  - DOI:10.1038/s41594-024-01399-z
UR  - https://juser.fz-juelich.de/record/1031787
ER  -