Structure, function and assembly of nuclear pore complexes

Abstract

The defining property of eukaryotic cells is the storage of heritable genetic material in a nuclear compartment. For eukaryotic cells to carry out the myriad biochemical processes necessary for their function, macromolecules must be efficiently exchanged between the nucleus and cytoplasm. The nuclear pore complex (NPC) — which is a massive assembly of ~35 different proteins present in multiple copies totalling ~1,000 protein subunits and architecturally conserved across eukaryotes — establishes a size-selective channel for regulated bidirectional transport of folded macromolecules and macromolecular assemblies across the nuclear envelope. In this Review, we provide an overview of insights gained from recent near-atomic composite structures of the NPC and their importance in advancing our understanding of NPC function. We discuss advances in our understanding of the permeability barrier, modes of nucleocytoplasmic transport, and the mobile transport factors involved. Finally, we present future research directions aimed at elucidating the nuclear basket architecture, mechanisms of mRNA export, NPC biogenesis and mechanosensation.