Some nuclear export signals (NESs) bind to the transport receptor CRM1 in the opposite orientation to those previously studied.

The ciliary G-protein Arl13B – which is often mutated in Joubert syndrome – is the Guanine nucleotide exchange factor for the G-protein Arl3 and exclusively localizes to cilia.

First systemic lysosomal proteomes in association with longevity and tissue specificity in C. elegans uncover lysosomal heterogeneity across multiple scales and provide valuable resources for understanding how lysosomes modulate signal transduction, organelle communication, tissue physiology, and organism longevity.

A key role for RNAs in sensing and mounting a response to mitochondrial stress.

Building on previous work (Fung et al., 2015), the structures of eight new nuclear export signal (NES) peptides bound to Exportin CRM1 are reported, revealing striking diversity in NES structures, a small conserved secondary structural element, and a CRM1 residue that functions as a selectivity filter.

A refined analysis of the mechanisms controlling CaM kinase-1 subcellular localization in sensory neurons, a cell-autonomous process known to control nociceptive plasticity and to adjust avoidance behaviors.

Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.

Polarized fluorescence microscopy of individual nuclear pores in vivo reveals conformational changes in select domains of proteins of the inner ring.

Animal RanBP1 nuclear export and cargo dissociation mechanisms are surprisingly different from yeast, due to mutations of critical residues, leading to greater nuclear transport efficiency and higher energy cost.

A new resource quantifying the distribution of 5,000 individual proteins between nucleus and cytoplasm, as well as identifying 2,800 yeast, human and frog proteins that are exported from the nucleus by the exportin CRM1/Xpo1.