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Targeting of Nbp1 to the inner nuclear membrane is essential for spindle pole body duplication

Spindle pole bodies (SPBs), like nuclear pore complexes, are embedded in the nuclear envelope (NE) at sites of fusion of the inner and outer nuclear membranes. A network of interacting proteins is required to insert a cytoplasmic SPB precursor into the NE. A central player of this network is Nbp1 th...

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Main Authors: Kupke, Thomas (Author) , Di Cecco, Leontina (Author) , Müller, Hans-Michael (Author) , Neuner, Annett (Author) , Adolf, Frank (Author) , Wieland, Felix T. (Author) , Nickel, Walter (Author) , Schiebel, Elmar (Author)
Format: Article (Journal)
Language:English
Published: 22 July 2011
In: The EMBO journal
Year: 2011, Volume: 30, Issue: 16, Pages: 3337-3352
ISSN:1460-2075
DOI:10.1038/emboj.2011.242
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/emboj.2011.242
Verlag, lizenzpflichtig, Volltext: https://www.embopress.org/doi/full/10.1038/emboj.2011.242
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Author Notes:Thomas Kupke, Leontina Di Cecco, Hans-Michael Müller, Annett Neuner, Frank Adolf, Felix Wieland, Walter Nickel and Elmar Schiebel
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Summary:Spindle pole bodies (SPBs), like nuclear pore complexes, are embedded in the nuclear envelope (NE) at sites of fusion of the inner and outer nuclear membranes. A network of interacting proteins is required to insert a cytoplasmic SPB precursor into the NE. A central player of this network is Nbp1 that interacts with the conserved integral membrane protein Ndc1. Here, we establish that Nbp1 is a monotopic membrane protein that is essential for SPB insertion at the inner face of the NE. In vitro and in vivo studies identified an N-terminal amphipathic α-helix of Nbp1 as a membrane-binding element, with crucial functions in SPB duplication. The karyopherin Kap123 binds to a nuclear localization sequence next to this amphipathic α-helix and prevents unspecific tethering of Nbp1 to membranes. After transport into the nucleus, Nbp1 binds to the inner nuclear membrane. These data define the targeting pathway of a SPB component and suggest that the amphipathic α-helix of Nbp1 is important for SPB insertion into the NE from within the nucleus.
Item Description:Gesehen am 11.07.2022
Physical Description:Online Resource
ISSN:1460-2075
DOI:10.1038/emboj.2011.242

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