Anti-colocalization of EXP2 and PfNCR1. (a) Center confocal slice and Mollweide projections of PfNCR1-GFP—EXP2-mRuby3 parasites. EXP2-mRuby3 (top, magenta), PfNCR1-GFP (middle, green), merge (bottom). Samples chosen represent examples of relatively low (0.48), average (−0.09) and high (−0.55) anti-correlation according to the Pearson correlation coefficients of the maps. The dotted line labels the equator, corresponds to the confocal slice. Scale bar: 1 µm. (C) Localization of EXP2 correlates with the existence of a relatively large PV lumen. The PV lumen can store proteins for export and accessory proteins to facilitate protein export. The lipid transporter PfNCR1 localizes to regions of close PPM-PVM apposition. Functionally, PfNCR1 may be able to directly contact the PVM to exchange lipids and sites of membrane apposition may be sites for the general exchange of lipophilic material, a functional hallmark of membrane contact sites.
Garten M, Beck JR, Roth R, Tenkova-Heuser T, Heuser J, Istvan ES, Bleck CKE, Goldberg DE, Zimmerberg J. Contacting domains segregate a lipid transporter from a solute transporter in the malarial host-parasite interface. Nat Commun. 2020 11(1):3825.
Other associated proteins
|PF3D7_0107500||Niemann-Pick type c1-related protein|