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Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly
Author(s) -
Vollmer Benjamin,
Schooley Allana,
Sachdev Ruchika,
Eisenhardt Nathalie,
Schneider Anna M,
Sieverding Cornelia,
Madlung Johannes,
Gerken Uwe,
Macek Boris,
Antonin Wolfram
Publication year - 2012
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2012.256
Subject(s) - nuclear pore , biology , nucleoporin , nucleoplasm , microbiology and biotechnology , nuclear lamina , cytoplasm , membrane , inner membrane , integral membrane protein , membrane protein , nuclear membrane , nuclear transport , biophysics , nuclear protein , biochemistry , cell nucleus , nucleolus , transcription factor , gene
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.