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- W4229443373 endingPage "5274" @default.
- W4229443373 startingPage "5274" @default.
- W4229443373 abstract "Mitochondria import about 1000 precursor proteins from the cytosol. The translocase of the outer membrane (TOM complex) forms the major entry site for precursor proteins. Subsequently, membrane-bound protein translocases sort the precursor proteins into the outer and inner membrane, the intermembrane space, and the matrix. The phospholipid composition of mitochondrial membranes is critical for protein import. Structural and biochemical data revealed that phospholipids affect the stability and activity of mitochondrial protein translocases. Integration of proteins into the target membrane involves rearrangement of phospholipids and distortion of the lipid bilayer. Phospholipids are present in the interface between subunits of protein translocases and affect the dynamic coupling of partner proteins. Phospholipids are required for full activity of the respiratory chain to generate membrane potential, which in turn drives protein import across and into the inner membrane. Finally, outer membrane protein translocases are closely linked to organellar contact sites that mediate lipid trafficking. Altogether, intensive crosstalk between mitochondrial protein import and lipid biogenesis controls mitochondrial biogenesis." @default.
- W4229443373 created "2022-05-11" @default.
- W4229443373 creator A5061242251 @default.
- W4229443373 creator A5074567235 @default.
- W4229443373 date "2022-05-09" @default.
- W4229443373 modified "2023-10-09" @default.
- W4229443373 title "Crosstalk between Mitochondrial Protein Import and Lipids" @default.
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