The Nup153-Nup50 protein interface and its role in nuclear import

Masaki Makise, Douglas R. Mackay, Suzanne Elgort, Sunita S. Shankaran, Stephen A. Adam, Katharine S. Ullman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)38515-38522
Number of pages8
JournalJournal of Biological Chemistry
Issue number46
StatePublished - Nov 9 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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