Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex

Hyuk Soo Seo, Yingli Ma, Erik W. Debler, Daniel Wacker, Stephan Kutik, Günter Blobel, André Hoelz

Research output: Contribution to journalArticlepeer-review

65 Scopus citations

Abstract

The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a β propeller and an α-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC.

Original languageEnglish
Pages (from-to)14281-14286
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number34
DOIs
StatePublished - 25 Aug 2009
Externally publishedYes

Keywords

  • Crystal structure
  • Fluorescence localization
  • Nuclear pore complex
  • Site-directed mutagenesis
  • mRNA export

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