TY  - JOUR
A1  - Theis, Jasmine
A1  - Gupta, Tilak Kumar
A1  - Klingler, Johannes
A1  - Wan, William
A1  - Albert, Sahradha
A1  - Keller, Sandro
A1  - Engel, Benjamin D.
A1  - Schroda, Michael
T1  - VIPP1 rods engulf membranes containing phosphatidylinositol phosphates
T2  - Scientific Reports
N2  - In cyanobacteria and plants, VIPP1 plays crucial roles in the biogenesis and repair of thylakoid membrane protein complexes and in coping with chloroplast membrane stress. In chloroplasts, VIPP1 localizes in distinct patterns at or close to envelope and thylakoid membranes. In vitro, VIPP1 forms higher-order oligomers of >1 MDa that organize into rings and rods. However, it remains unknown how VIPP1 oligomerization is related to function. Using time-resolved fluorescence anisotropy and sucrose density gradient centrifugation, we show here that Chlamydomonas reinhardtii VIPP1 binds strongly to liposomal membranes containing phosphatidylinositol-4-phosphate (PI4P). Cryo-electron tomography reveals that VIPP1 oligomerizes into rods that can engulf liposomal membranes containing PI4P. These findings place VIPP1 into a group of membrane-shaping proteins including epsin and BAR domain proteins. Moreover, they point to a potential role of phosphatidylinositols in directing the shaping of chloroplast membranes.
Y1  - 2019
UR  - https://kluedo.ub.uni-kl.de/frontdoor/index/index/docId/5829
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:386-kluedo-58294
SN  - 2045-2322
IS  - 9, 8725 (2019)
PB  - Springer Nature - Nature Publishing Group
ER  -