Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly

被引:13
|
作者
Hamed, Mohamed [1 ]
Antonin, Wolfram [1 ]
机构
[1] Rhein Westfal TH Aachen, Inst Biochem & Mol Cell Biol, Sch Med, D-52074 Aachen, Germany
关键词
amphipathic helix; ALPS motif; membrane curvature; Nup155; Nup53; Y-complex; Nup153; MESSENGER-RNA EXPORT; INTEGRATIVE STRUCTURE; CELL-DIFFERENTIATION; NUP107-160; COMPLEX; CRYSTAL-STRUCTURE; VESICLE COATS; PROTEIN; YEAST; ARCHITECTURE; CURVATURE;
D O I
10.3390/cells10123601
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
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页数:17
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