Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
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DOI:
10.1038/emboj.2012.256
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发表时间:
2012-10-17
期刊:
影响因子:
11.4
通讯作者:
Antonin, Wolfram
中科院分区:
文献类型:
--
作者:
Vollmer, Benjamin;Schooley, Allana;Sachdev, Ruchika;Eisenhardt, Nathalie;Schneider, Anna M.;Sieverding, Cornelia;Madlung, Johannes;Gerken, Uwe;Macek, Boris;Antonin, Wolfram
Nuclear pore complexes (NPCs) fuse the two membranes of the nuclear envelope (NE) to a pore, connecting cytoplasm and nucleoplasm and allowing exchange of macromolecules between these compartments. Most NPC proteins do not contain integral membrane domains and thus it is largely unclear how NPCs are embedded and anchored in the NE. Here, we show that the evolutionary conserved nuclear pore protein Nup53 binds independently of other proteins to membranes, a property that is crucial for NPC assembly and conserved between yeast and vertebrates. The vertebrate protein comprises two membrane binding sites, of which the C-terminal domain has membrane deforming capabilities, and is specifically required for de novo NPC assembly and insertion into the intact NE during interphase. Dimerization of Nup53 contributes to its membrane interaction and is crucial for its function in NPC assembly.
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影响因子:
9.8
作者:
Devos D;Dokudovskaya S;Alber F;Williams R;Chait BT;Sali A;Rout MP
通讯作者:
Rout MP
DOI:
10.1074/mcp.m900038-mcp200
发表时间:
2009-09
期刊:
Molecular & cellular proteomics : MCP
影响因子:
--
作者:
DeGrasse JA;DuBois KN;Devos D;Siegel TN;Sali A;Field MC;Rout MP;Chait BT
通讯作者:
Chait BT
DOI:
10.1083/jcb.200806174
发表时间:
2009-03-09
期刊:
The Journal of cell biology
影响因子:
--
作者:
Dawson TR;Lazarus MD;Hetzer MW;Wente SR
通讯作者:
Wente SR
影响因子:
16.8
作者:
Drin, Guillaume;Casella, Jean-Francois;Antonny, Bruno
通讯作者:
Antonny, Bruno
影响因子:
7.8
作者:
Anderson, Daniel J.;Hetzer, Martin W.
通讯作者:
Hetzer, Martin W.