Transport receptors articles from across Nature Portfolio

The HIV-1 capsid behaves like a nuclear transport receptor entering and traversing an FG phase, with its interior serving as a cargo container, bypassing an otherwise effective barrier to viral infection.

Nuclear transport receptors mediate nucleocytoplasmic transport, collectively termed karyopherin-β (Kap-β) in yeast. Here, the authors present a cryo-EM structure of Kap114p, one of the Kap-βs, revealing a non-canonical function beyond nuclear transport that modulates yTBP-dependent transcription.

Importins are known to facilitate nucleocytoplasmic transport and cytoplasmic chaperoning of some proteins. Here, the authors uncover that these proteins also act as co-translational chaperones for specific sets of proteins, for example ribonucleic acid binding factors.

Nuclear translocation of the p50/p65 heterodimer is essential for NF-κB signaling. Here, the authors identify a bipartite Nuclear Localization Signal in the NF-κB p50/p65 heterodimer that is recognized with high affinity by importin α3.

The majority of macromolecules are transported across the nuclear membrane by the Karyopherin-β (Kap) proteins, comprising importins, exportins and biportins. Unravelling mechanisms and regulation of Kap–cargo interactions is essential for understanding nuclear export and import of proteins and RNA and how this traffic impacts their physiological functions.

Importin superfamily member IPO13 mediates nuclear transport bidirectionally. Here the authors delineate the transcriptome of wild-type and IPO13-knockout mouse embryonic stem cells, revealing IPO13’s key role in the oxidative stress response through targeted transport of specific transcription factors.

Taylor et al. demonstrate a causative role for XPO1 mutations in cancer through changing nuclear export signal recognition.