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

Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10065, USA.

Proceedings of the National Academy of Sciences of the United States of America 2009 Aug 25

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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 beta propeller and an alpha-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.

Citation

Hyuk-Soo Seo, Yingli Ma, Erik W Debler, Daniel Wacker, Stephan Kutik, Günter Blobel, André Hoelz. Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex. Proceedings of the National Academy of Sciences of the United States of America. 2009 Aug 25;106(34):14281-6