Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion.
The photosynthetic light reaction takes place within the thylakoid membrane system in cyanobacteria and chloroplasts. Besides its global importance, the biogenesis, maintenance and dynamics of this membrane system are still a mystery. In the last two decades, strong evidence supported the idea that these processes involve IM30, the inner membrane-associated protein of 30kDa, a protein also known as the vesicle-inducing protein in plastids 1 (Vipp1). Even though we just only begin to understand the precise physiological function of this protein, it is clear that interaction of IM30 with membranes is crucial for biogenesis of thylakoid membranes. Here we summarize and discuss forces guiding IM30-membrane interactions, as the membrane properties as well as the oligomeric state of IM30 appear to affect proper interaction of IM30 with membrane surfaces. Interaction of IM30 with membranes results in an altered membrane structure and can finally trigger fusion of adjacent membranes, when Mg2+is present. Based on recent results, we finally present a model summarizing individual steps involved in IM30-mediated membrane fusion. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.
Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
Jennifer
J
Heidrich
Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
Adrien
A
Thurotte
Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany. Electronic address: Dirk.Schneider@uni-mainz.de.
Dirk
D
Schneider
D017360:Arabidopsis / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D002413:Cations, Divalent; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism; D008561:Membrane Fusion; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D001678:Organelle Biogenesis; D010743:Phospholipids / Q000737:chemistry* / Q000378:metabolism; D010788:Photosynthesis / Q000502:physiology; D059828:Plant Cells / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D055503:Protein Multimerization; D046939:Synechocystis / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D020524:Thylakoids / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D029681:Arabidopsis Proteins; D001426:Bacterial Proteins; D002413:Cations, Divalent; D008565:Membrane Proteins; D010743:Phospholipids; C424448:VIPP1 protein, Arabidopsis; C424449:VIPP1 protein, Synechocystis; D008274:Magnesium
Chloroplasts; Cyanobacteria; IM30; PspA; Thylakoid membrane biogenesis; Vipp1