Publications by authors named "R E Voorhees"
Article Synopsis
- Mitochondrial function relies on properly positioned membrane proteins in the outer mitochondrial membrane, which features around 150 proteins predominantly made up of α-helical transmembrane domains.
- The expansion of this family of proteins in metazoans is crucial for various processes like mitochondrial fusion, fission, and immune responses, highlighted by the role of MTCH2 as an important insertase.
- The text introduces three experimental methods to study α-helical protein insertion: a split fluorescent reporter system for live cell monitoring, an approach for isolating functional mitochondria for lab assays, and a technique for reconstituting protein insertion using proteoliposomes with MTCH2, paving the way for deeper analysis of mitochondrial protein dynamics.
Mammalian membrane proteins perform essential physiologic functions that rely on their accurate insertion and folding at the endoplasmic reticulum (ER). Using forward and arrayed genetic screens, we systematically studied the biogenesis of a panel of membrane proteins, including several G-protein-coupled receptors (GPCRs). We observed a central role for the insertase, the ER membrane protein complex (EMC), and developed a dual-guide approach to identify genetic modifiers of the EMC.
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- Mitochondrial outer membrane α-helical proteins are essential for communication between mitochondria and the cytoplasm, but their targeting and insertion processes are not fully understood.
- A study using genome-wide CRISPRi screens identified key factors involved in the biogenesis of these proteins, revealing distinct pathways based on the proteins' topology.
- Specific components like NAC and TTC1 play critical roles in how different types of membrane proteins are targeted and inserted, with TTC1 acting as a chaperone that aids in the solubilization and insertion of signal-anchored proteins into the mitochondria.
Mammalian membrane proteins perform essential physiologic functions that rely on their accurate insertion and folding at the endoplasmic reticulum (ER). Using forward and arrayed genetic screens, we systematically studied the biogenesis of a panel of membrane proteins, including several G-protein coupled receptors (GPCRs). We observed a central role for the insertase, the ER membrane protein complex (EMC), and developed a dual-guide approach to identify genetic modifiers of the EMC.
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