Nuclear pore complex proteins.
The nuclear envelope forms the boundary between the nucleus and the cytoplasm and as such regulates the exchange of macromolecules between the two compartments. The channels through the nuclear envelop that actually mediate this macromolecular traffic are the nuclear pore complexes. These are extremely elaborate structures which in vertebrate cells exhibit a mass of approximately 120 MDa. They are thought to be composed of as many as 100 distinct polypeptide subunits. A major challenge in the field of nucleocytoplasmic transport is to identify these subunits and to determine their functions and interactions in the context of the three-dimensional structure of the nuclear pore complex. It is the aim of this review to summarize what is currently known of the 20 or so nuclear pore complex proteins that have been described in either vertebrate or yeast cells.
Bastos
R
R
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Panté
N
N
Burke
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006023:Glycoproteins; D006801:Humans; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D009687:Nuclear Proteins / Q000737:chemistry / Q000502:physiology
D006023:Glycoproteins; D009687:Nuclear Proteins