biostudies-literatureGachie SWKAKENHICollaborative Research Program of Institute for Protein Research, Osaka UniversityMinistry of Education, Culture, Sports, Science and TechnologyJapan Society for the Promotion of Sciencekiaf137https://www.ebi.ac.uk/biostudies/studies/S-EPMC12043068biostudies-literatureUnknown198(1)The thylakoid membrane (TM) serves as the scaffold for oxygen-evolving photosynthesis, hosting the protein complexes responsible for the light reactions and ATP synthesis. Vesicle inducing protein in plastid 1 (VIPP1), a key protein in TM remodeling, has been recognized as essential for TM homeostasis. In vitro studies of cyanobacterial VIPP1 demonstrated its ability to form large homo-oligomers (2 MDa) manifesting as ring-like or filament-like assemblies associated with membranes. Similarly, VIPP1 in Chlamydomonas reinhardtii assembles into rods that encapsulate liposomes or into stacked spiral structures. However, the nature of VIPP1 assemblies in chloroplasts, particularly in Arabidopsis, remains uncharacterized. Here, we expressed Arabidopsis thaliana VIPP1 fused to GFP (AtVIPP1-GFP) iPlant physiologyThe thylakoid membrane remodeling protein VIPP1 forms bundled oligomers in tobacco chloroplasts.PMC1204306823H0495921H02508CR-24-02Yoshimura RTerachi TLi DGoto YGachie SWZhang LTakami TSakamoto WKawamoto AMuhire ATakeda-Kamiya NSato MKurisu GToyooka KfalseThe thylakoid membrane remodeling protein VIPP1 forms bundled oligomers in tobacco chloroplasts.The thylakoid membrane (TM) serves as the scaffold for oxygen-evolving photosynthesis, hosting the protein complexes responsible for the light reactions and ATP synthesis. Vesicle inducing protein in plastid 1 (VIPP1), a key protein in TM remodeling, has been recognized as essential for TM homeostasis. In vitro studies of cyanobacterial VIPP1 demonstrated its ability to form large homo-oligomers (2 MDa) manifesting as ring-like or filament-like assemblies associated with membranes. Similarly, VIPP1 in Chlamydomonas reinhardtii assembles into rods that encapsulate liposomes or into stacked spiral structures. However, the nature of VIPP1 assemblies in chloroplasts, particularly in Arabidopsis, remains uncharacterized. Here, we expressed Arabidopsis thaliana VIPP1 fused to GFP (AtVIPP1-GFP) i2025-01-01T00:00:00Z2025 Apr2025-06-25T03:06:31.398Z2025-06-25T03:06:31.398ZS-EPMC120430684019887110.1093/plphys/kiaf137