| Literature DB >> 23007389 |
Masaki Makise1, Douglas R Mackay, Suzanne Elgort, Sunita S Shankaran, Stephen A Adam, Katharine S Ullman.
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.Entities:
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Year: 2012 PMID: 23007389 PMCID: PMC3493896 DOI: 10.1074/jbc.M112.378893
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157