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Structure of human mitochondrial pyruvate carrier MPC1 and MPC2 complex - Nature Communications
Abstract The Mitochondrial Pyruvate Carrier (MPC) bridges cytosolic and mitochondrial metabolism by transporting pyruvate into mitochondria for ATP production and biosynthesis of various essential molecules. MPC functions as a heterodimer composed of MPC1 and MPC2 in most mammalian cells.
The cytosolic N-terminal domain of V-ATPase a-subunits is a regulatory hub targeted by multiple signals
Farzana Tuli and Patricia M. Kane* Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, United States Vacuolar H+-ATPases (V-ATPases) acidify several organelles in all eukaryotic cells and export protons across the plasma membrane in a subset of cell types. V-ATPases are multisubunit enzymes consisting of a peripheral subcomplex, V1, that is exposed to the cytosol and an integral membrane subcomplex, Vo, that contains the proton pore.
Structure of nevanimibe-bound tetrameric human ACAT1
Abstract Cholesterol is an essential component of mammalian cell membranes, constituting up to 50% of plasma membrane lipids. By contrast, it accounts for only 5% of lipids in the endoplasmic reticulum (ER)1. The ER enzyme sterol O-acyltransferase 1 (also named acyl-coenzyme A:cholesterol acyltransferase, ACAT1) transfers a long-chain fatty acid to cholesterol to form cholesteryl esters that coalesce into cytosolic lipid droplets.
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