Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.
The conformational mechanism of a transporter protein is found to have profound and energetically costly effects on the morphology of the surrounding membrane.
Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.
Carbonic anhydrase II features a surface proton antenna that exclusively mediates proton exchange with monocarboxylate transporters to facilitate proton-coupled lactate transport in cancer cells.
CRISPR/Cas knockout of intraflagellar transport protein 80 shows that this subunit is absolutely required for ciliogenesis, and biophysical studies reveal that this protein may dimerize the intraflagellar transport complex.
A novel regulatory step in the endocytic pathway, which occurs post-internalization, takes place at the trans-Golgi network and involves the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5.
Selective import via bacterial ABC importers is facilitated by a hitherto unrecognized complexity in the conformational dynamics of the substrate-binding proteins.
The conserved polypeptide transport associated (POTRA) domains of the protein import channel, Toc75, are essential for protein import into chloroplasts.
