The Nup153-Nup50 Protein Interface and Its Role in Nuclear Import |
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Authors: | Masaki Makise Douglas R Mackay Suzanne Elgort Sunita S Shankaran Stephen A Adam Katharine S Ullman |
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Institution: | From the ‡Department of Oncological Sciences, University of Utah, Salt Lake City, Utah 84112.;the §Faculty of Pharmaceutical Sciences, Sojo University, Kumamoto 860-0082, Japan, and ;the ¶Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611 |
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Abstract: | Interactions between Nup50 and soluble transport factors underlie the efficiency of certain nucleocytoplasmic transport pathways. The platform on which these interactions take place is important to building a complete understanding of nucleocytoplasmic trafficking. Nup153 is the nucleoporin that provides this scaffold for Nup50. Here, we have delineated requirements for the interaction between Nup153 and Nup50, revealing a dual interface. An interaction between Nup50 and a region in the unique N-terminal region of Nup153 is critical for the nuclear pore localization of Nup50. A second site of interaction is at the distal tail of Nup153 and is dependent on importin α. Both of these interactions involve the N-terminal domain of Nup50. The configuration of the Nup153-Nup50 partnership suggests that the Nup153 scaffold provides not just a means of pore targeting for Nup50 but also serves to provide a local environment that facilitates bringing Nup50 and importin α together, as well as other soluble factors involved in transport. Consistent with this, disruption of the Nup153-Nup50 interface decreases efficiency of nuclear import. |
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Keywords: | Cell Biology Nuclear Membrane Nuclear Pore Nuclear Transport Nucleus Npap60 Nup153 Nup50 Nuclear Pore Complex Nucleocytoplasmic Transport |
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