Genetic finding of pathogenic CRMP1 variants in three unrelated individuals with neurodevelopmental disorder, supported by structural simulation, biochemical and proof-of-principle data highlights the key role of CRMP1 in the development and functioning of the nervous system in humans.

CRMP4 is a new actor in the guidance cue Semaphorin-3E pathway, crucially involved in the establishment of the fornix, a key axonal tract for memory and emotional control.

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

Nup98-HoxA9 is recruited to Hox gene cluster regions together with the chromosomally pre-bound nuclear export factor Crm1, which induces aberrant expression of several Hox genes and affecting the differentiation of embryonic stem cells.

A key molecule that connects leukemogenic proteins to aberrant HOX gene regulation turned out to be a nuclear export factor, CRM1.

The nuclear export receptor Crm1 cooperatively binds its HIV Rev-RRE cargo as a dimer using a species-specific interface that supports viral replication by enhancing nuclear export of HIV RNA.

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.

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.

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.