, Volume 115, Issue 2, pp 98-109
Date: 19 Jan 2006

Nuclear transport is becoming crystal clear

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In the more than 30 years since the field of nucleocytoplasmic transport first emerged, transport processes have been studied extensively using a combination of biochemical, cell biological, and genetic techniques. All soluble transport receptors of the importin-β family of karyopherins have been identified by sequence homology, and most have been functionally characterized in various model systems. In addition, biochemical purifications have led to the identification of what is likely every bona fide component of the nuclear pore complex (NPC), the nuclear envelope-embedded channel that mediates all nuclear transport events (Cronshaw et al. 2002; Rout et al. 2000). Now that the majority of the proteins involved in nuclear transport are known, the focus of research is shifting to mechanistic questions of nuclear pore function and regulation of transport events. In recent years, we have seen a flurry of papers that look closely at the high-resolution molecular structures and interaction

Communicated by E. A. Nigg