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

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.

Slx9 is a newly discovered type of RanGTP-binding protein required for Crm1-mediated nuclear export.

Cellular and genetic approaches reveal that exposure of a normally buried nuclear export signal (NES)-like sequence mediates export of ALS-linked mutant and misfolded wild-type SOD1 to the cytoplasm by CRM1.

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.

Gαq stimulates HDAC5 phosphorylation by PKC-independent PKD/PKCμ activation to induce the IκB expression and limit the NF-κB-mediated inflammatory response which essential for proper endometrial decidualization and early pregnancy.

Human GDOWN1 is identified as an extremely tightly controlled nucleocytoplasmic shuttling protein, and its translocation into the nucleus plays a crucial role in modulating the global transcription and facilitating the cellular adaptation to certain stresses.

A comprehensive analysis of yeast mutants has provided clues to understanding the physiological conditions caused by protein overexpression.

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.

Within the nucleus, Dbp5p supports tRNA export providing a parallel mechanism by which this conserved DEAD-box protein functions to support eukaryotic gene expression.