The nuclear pore complex (NPC) creates an aqueous channel across the n
uclear envelope through which macromolecular transport between nucleus
and cytoplasm occurs, Nucleocytoplasmic traffic is bidirectional and
involves diverse substrates, including protein and RNA, It is unclear
whether import and export ate mechanistically similar, but evidence su
ggests that numerous pathways may be involved, The discovery of filame
nts that extend out from each side of the NPC suggests that the NPC ma
y also have a structural role, perhaps providing a connection between
cytoskeletal elements of the nucleus and cytoplasm. If this suggestion
is valid, it remains to be determined whether this aspect of NPC func
tion is related to its role in nuclear transport. This review discusse
s recent development regarding the structure of the NPC, characterizat
ion of its constituent proteins (nucleoporins), the mechanism by which
transport occurs, the function of individual nucleoporins, and the pa
thway of NPC assembly and disassembly.