R.M. Voorhees

The paper identifies FAM136A as a chaperone essential for mitochondrial membrane protein biogenesis, specifically for VDAC paralogs and some electron transport chain subunits.

The paper identifies MTCH2 as a defining member of a conserved mitochondrial outer membrane insertase family and reveals structural features essential for its function across eukaryotes.

The paper identifies TXNDC15 as a regulator of ER membrane protein quality control, showing it modulates MARCHF6 to prevent degradation of critical ciliary proteins, thereby affecting ciliogenesis.

The paper shows that short disordered peptides can convert proteins into mechanosensors that respond to cellular forces, expanding the known mechanisms of mechanosensing.

The paper studies the biogenesis of ER membrane proteins, identifying the EMC and BOS complex as key players and proposing a model for coordinated insertion.

The paper introduces a dual sgRNA library design for CRISPRi screens to identify genetic modifiers, showing improved sensitivity and specificity in detecting epistatic relationships.

The paper identifies a targeted degradation pathway for nascent proteins from PTC-containing mRNAs, showing CNOT4's role in coupling NMD with protein quality control.

This study identifies WNK1 as an essential factor for EMC assembly by stabilizing EMC2 and preventing promiscuous interactions.

The paper investigates how the WRB/CAML complex regulates subunit assembly, finding two distinct pathways for correcting or degrading orphan subunits in the ER.