TL;DR: The best understood system for the transport of macromolecules between the cytoplasm and the nucleus is the classical nuclear import pathway and a bioinformatics approach is taken to analyze the likely prevalence of this system in vivo.
TL;DR: The crystal structure of a 50 kDa fragment of the 60 kDa yeast karyopherin alpha is reported, which reveals the determinants of NLS specificity and suggests a model for the recognition of bipartite NLSs.
TL;DR: It is proposed that movement of NLS proteins across the nuclear pore complex is a stochastic process that operates via repeated association-dissociation reactions.
TL;DR: Control mechanisms that importin α exerts over the assembly and disassembly of the ternary complex are discussed and how new groups of importinα genes arose during the evolution of metazoan animals to function in development and differentiation is described.
TL;DR: It is reported that the previously identified CAS protein mediates importin α re-export and binds preferentially to NLS-free Importin α, explaining why import substrates stay in the nucleus.