Exportin 6 (XPO6)

Exportins, such as XPO6, recruit cargo in the nucleoplasm in the presence of RAN-GTP and form ternary export complexes. These complexes are transported through nuclear pore complexes to the cytoplasm, where GTP is hydrolyzed and the export complex is disassembled.

The preferred cargo was the profilin-actin complex, since XPO6 showed little or no binding to either protein in the absence of the other. Analysis of the weak interaction between XPO6 and isolated actin suggested that XPO6 bound the complex via association with the actin component. Knockdown of Drosophila Exp6 by RNA interference abolished nuclear exclusion of actin and resulted in the appearance of nuclear actin paracrystals.