Letter abstract
Nature Cell Biology 9, 788 - 796 (2007)
Published online: 3 June 2007 | doi:10.1038/ncb1604
Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex
Philipp Stelter1, Ruth Kunze1, Dirk Flemming1, Dominic Höpfner2, Meikel Diepholz3, Peter Philippsen2, Bettina Böttcher3 & Ed Hurt1
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope1. Here, we discovered an unexpected role for yeast dynein light chain (Dyn2)2 in the NPC. Dyn2 is a previously undescribed nucleoporin that functions as molecular glue to dimerize and stabilize the Nup82–Nsp1–Nup159 complex, a module of the cytoplasmic pore filaments3. Biochemical analyses showed that Dyn2 binds to a linear motif (termed DIDNup159) inserted between the Phe-Gly repeat and coiled-coil domain of Nup159. Electron microscopy revealed that the reconstituted Dyn2–DIDNup159 complex forms a rigid rod-like structure, in which five Dyn2 homodimers align like 'pearls on a string' between two extented DIDNup159 strands. These findings imply that the rigid 20 nm long Dyn2–DIDNup159 filament projects the Nup159 Phe-Gly repeats from the Nup82 module. Thus, it is possible that dynein light chain plays a role in organizing natively unfolded Phe-Gly repeats within the NPC scaffold to facilitate nucleocytoplasmic transport.
- Biochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
- Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland.
- EMBL, Meyerhofstrase 1, D-69117 Heidelberg, Germany.
Correspondence to: Ed Hurt1 e-mail: ed.hurt@bzh.uni-heidelberg.de
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