SCYL1

SCYL1 is the founding member of the SCY1-like family, combining an N-terminal protein-kinase-like domain that functions as a pseudokinase with C-terminal tetratricopeptide-repeat-like motifs. It localizes to the cytoplasmic face of the nuclear pore and partners with RanBP2 in a complex implicated in nuclear export of selected cargos, including histone mRNAs and certain viral proteins. Although SCYL1 lacks robust catalytic activity, it contributes structurally to nucleocytoplasmic transport and Golgi organization. Biallelic SCYL1 mutations cause a human syndrome of spinocerebellar ataxia with episodic liver dysfunction and peripheral neuropathy. Recombinant SCYL1 aids studies of nuclear-pore-associated transport and this rare neurodegenerative disorder.