Abstract
Nuclear pore complexes (NPCs) mediate the selective and highly efficient transport between the cytoplasm and the nucleus. They are embedded in the two membrane structure of the nuclear envelope at sites where these two membranes are fused to pores. A few transmembrane proteins are an integral part of NPCs and thought to anchor these complexes in the nuclear envelope. In addition, a number of nucleoporins without membrane spanning domains interact with the pore membrane. Here we review our current knowledge of how these proteins interact with the membrane and how this interaction can contribute to NPC assembly, stability and function as well as shaping of the pore membrane.
Highlights
Nuclear pore complexes (NPCs) are the gatekeepers of the nucleus
Depending on whether cells break down their nuclear envelope during mitosis or not, different modes of NPC assembly exist: animal cells typically proceed via an open mitosis and disassemble the nuclear envelope, at least partially, with entry into mitosis and reassemble the nuclear envelope after successful chromatin segregation
The NPC protein network contacts the pore membrane at numerous sites, often via amphipathic helixes that insert into one lipid leaflet of the membrane
Summary
Nuclear pore complexes (NPCs) are the gatekeepers of the nucleus. They control the flux of molecules across the nuclear envelope, consisting of an outer and inner nuclear membrane, and establish the identity of the nucleus and cytoplasm as distinct compartments. In Saccharomyces cerevisiae, the approximate mass of 65 MDa is smaller but still considerable In spite of their enormous size, NPCs are composed of about only 30 different proteins called nucleoporins (Figure 1), which are all present in multiple copies in these assemblies. The proto-coatomer hypothesis states that these nucleoporins act as NPC coats on the pore membrane and are, along with vesicle coating proteins, derived from a common ancestral membrane shaping unit [8,10,11] This is further corroborated by proteins moonlighting between different coating functions such as Sec or Seh, which are part of both the NPCs and the COPII or the SEA complex, a vacuolar membrane coat in yeast species. A number of nucleoporins show direct membrane binding and we will review here how they contribute to NPC structure and its assembly
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