Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly
Open Access
- 7 September 2012
- journal article
- Published by Springer Science and Business Media LLC in The EMBO Journal
- Vol. 31 (20), 4072-4084
- https://doi.org/10.1038/emboj.2012.256
Abstract
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.Keywords
This publication has 63 references indexed in Scilit:
- 3D ultrastructure of the nuclear pore complexCurrent Opinion in Cell Biology, 2012
- Insight into Structure and Assembly of the Nuclear Pore Complex by Utilizing the Genome of a Eukaryotic ThermophileCell, 2011
- Nuclear pore complex—a coat specifically tailored for the nuclear envelopeCurrent Opinion in Cell Biology, 2011
- Cell Cycle-Dependent Differences in Nuclear Pore Complex Assembly in MetazoaCell, 2010
- Evidence for a Shared Nuclear Pore Complex Architecture That Is Conserved from the Last Common Eukaryotic AncestorMolecular & Cellular Proteomics, 2009
- Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cellsThe Journal of cell biology, 2008
- Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substratesProceedings of the National Academy of Sciences, 2008
- MEL‐28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assemblyEMBO Reports, 2007
- ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell divisionProceedings of the National Academy of Sciences, 2006
- Specific Binding of the Karyopherin Kap121p to a Subunit of the Nuclear Pore Complex Containing Nup53p, Nup59p, and Nup170pThe Journal of cell biology, 1998