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Serine/arginine-rich (SR) proteins constitute a class of splicing regulators in plants and animals. Tillemans et al. (pages 3218–3234) investigated the nuclear localization of different domain-deleted mutant proteins of the Arabidopsis SR splicing factor RSZp22, a homolog of the human 9G8 splicing factor. The authors show that nucleolar localization of RSZp22 involves different domains or motifs, and the mobility of SR proteins between different nuclear territories depends on the cellular phosphorylation state. The results further suggest that RSZp22 is a nucleocytoplasmic shuttling protein. This work emphasizes the high mobility of Arabidopsis SR splicing factors and provides insights into the dynamic relationships between the different nuclear compartments. The cover shows Z-series confocal images of a nucleus expressing RSZp22-GFP following treatment with leptomycin B, demonstrating the concentration of the fusion protein in intranuclear domains after inhibition of the CRM1/exportin1 nuclear export pathway (the concentration of RSZp22-GFP is depicted with various pseudocolor images).