Bastos R, Panté N, Burke B
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Int Rev Cytol. 1995;162B:257-302. doi: 10.1016/s0074-7696(08)62619-4.
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.
核膜形成了细胞核与细胞质之间的边界，因此调节着两个区室之间大分子的交换。穿过核膜实际介导这种大分子运输的通道是核孔复合体。这些是极其复杂的结构，在脊椎动物细胞中质量约为120兆道尔顿。它们被认为由多达100个不同的多肽亚基组成。核质运输领域的一个主要挑战是鉴定这些亚基，并在核孔复合体的三维结构背景下确定它们的功能和相互作用。本综述的目的是总结目前已知的在脊椎动物或酵母细胞中描述的约20种核孔复合体蛋白。
