The envelope stress factor DolP associates with the outer membrane protein assembly machinery and supports proper folding and functioning of BamA contributing to preserve envelope integrity.
A combination of cryo-electron microscopy, structure prediction, and evolutionary analyses reveal several functional states of the dynamic protein translocation machinery at the mammalian endoplasmic reticulum.
John P O'Donnell, Ben P Phillips ... Ramanujan S Hegde
Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.
The protein translocation apparatus of the inner- (Sec) and outer-membrane (BAM) interact to form a trans-periplasmic super-complex capable of long-range, PMF-dependent conformational changes to facilitate efficient outer-membrane protein maturation.
A screen using artificially barcoded, exosomal microRNAs, paired with CRISPR guide RNAs, helped identify new players in multivesicular endosome exocytosis and a role for Wnt signaling.
Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.
The cotranslational membrane integration of three multispanning Escherichia coli inner membrane proteins is followed using force profile analysis, uncovering unexpected complexities in the membrane integration process.
A membrane protein complex in the endoplasmic reticulum is a key factor for the biogenesis of multi-pass transmembrane proteins, including Rh1, and its loss causes retinal degeneration.
