Protein translocation articles from across Nature Portfolio

Importin β, the prototypical eukaryotic nuclear import receptor, transports a wide variety of cargos into the nucleus. Ko et al. used cryogenic electron microscopy to reveal an unexpected allosteric regulation of Importin β’s affinity for FG-nucleoporins, triggered by Ran-GTP.

E3 ubiquitin ligase HRD1, a core component of the ER-associated degradation (ERAD) pathway, is essential for the TLR3-mediated innate immune response. HRD1 catalyzes polyubiquitination of TLR3 at lysine 813, which promotes its trafficking to endolysosomes and enables its proteolytic cleavage and functional activation.

The ciliary trafficking of EP4 is governed by a LPG motif in its C-terminal domain and the Rab23/IFT43 complex. These findings open a promising avenue for exploring the pathophysiological roles of ciliary EP4.

The authors identify TMEM145 as a critical protein in cochlear outer hair cells, responsible for linking their stereocilia. Mice lacking TMEM145 develop severe hearing loss at an early age, providing new insights into hearing loss mechanisms.

Bacteria of the phylum Bacteroidota move by gliding and export proteins using a type-9 secretion system. Here, Liu et al. show that these two processes use a shared mechanism in which outer membrane proteins are covalently attached by disulfide bonds to a moving track structure inside the cell.

Two seminal studies from the 1980s catalysed major advances in the trafficking field, when converging research in yeast and mammalian cells revealed the molecular machinery of the secretory pathway.

Two new studies find that HIV-1 can enter the nucleus by cracking or distorting nuclear pore structures, explaining how the HIV-1 capsid can seemingly ignore the size limitations associated with conventional nuclear import.

Blocking the translocase of the outer membrane (TOM) channel induces elimination of unoccupied protein import channels in the inner membrane by an ATP-dependent protease. Precursor-dependent adjustment of the number of translocator channels provides new insights into mitochondrial quality control upon protein import stress.