Related Experiment Video
Updated: Apr 4, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
Published on: March 11, 2011
Structural determinants of nuclear export signal orientation in binding to exportin CRM1
Ho Yee Joyce Fung1, Szu-Chin Fu1, Chad A Brautigam2
1Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, United States.
Abstract:
The Chromosome Region of Maintenance 1 (CRM1) protein mediates nuclear export of hundreds of proteins through recognition of their nuclear export signals (NESs), which are highly variable in sequence and structure. The plasticity of the CRM1-NES interaction is not well understood, as there are many NES sequences that seem incompatible with structures of the NES-bound CRM1 groove. Crystal structures of CRM1 bound to two different NESs with unusual sequences showed the NES peptides binding the CRM1 groove in the opposite orientation (minus) to that of previously studied NESs (plus). Comparison of minus and plus NESs identified structural and sequence determinants for NES orientation. The binding of NESs to CRM1 in both orientations results in a large expansion in NES consensus patterns and therefore a corresponding expansion of potential NESs in the proteome.
Related Concept Videos
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Nuclear Localization Signals and Import
Directionality of Nuclear Transport
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Regulation of Nuclear Protein Sorting
Nuclear Export of mRNA

