Membrane interactions of mitochondrial lipid transfer proteins

Abstract

The mitochondrial inner membrane is an integral part of the cellular lipid biosynthesis network. Intramitochondrial lipid transfer shuttles specific lipid species between the two mitochondrial membranes. This pathway is facilitated by designated protein complexes in the intermembrane space. A hetero-dimeric complex of Ups1 and Mdm35 has been identified in yeast to transfer phosphatidic acid from the outer to the inner membrane. Here, we define pH and lipid charge dependency of Ups1 membrane interaction. We show that Ups1 interacts with membranes in a membrane curvature dependent manner. Ups1 predominantly binds to membrane domains of positive curvature. Desorption of phosphatidic acid from positively curved membranes is energetically favorable over flat or negatively curved membranes. Hence, our results demonstrate that Ups1 specifically binds to membrane regions where extraction and insertion of lipids is enhanced.

Structural insights into crista junction formation by the Mic60-Mic19 complex

“…S1). These contact sites have been implicated, among others, in lipid transfer between the IMM and OMM ( 32 ). In this context, our structural data would support the idea of an arch dome-like assembly that vaults the entry into cristae.…”