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3. Nuclear pore complexes.

The nuclear pore complex (NPC) is huge macromolecular assembly (~30 different nucleoporins, ~50 MDa) in the nuclear envelope that transports cargo between the nucleus and cytoplasm. We study the NPC in yeast and apply genetic, biochemical ,cell biological and structural approaches to unravel the structure and function of this gigantic transport machine. Milestones in this research were the cloning of the first nucleoporin (termed Nsp1), the development of genetic screens on the basis of synthetic lethality to genetically dissect the NPC, the biochemical analysis of the NPC by using powerful affinity-purification methods for nucleoporins and NPC modules, the reconstitution of a seven-subunit containing NPC module and the discovery of a novel structural principle to generate higher order structures within the NPC scaffold with the identification of the dynein light chain as a molecular glue. Future studies involve the structural and functional analysis of the nuclear pore complex including reconstitution of NPC modules into the higher order NPC structure.

Philipp Stelter, Ruth Kunze, Monika Radwan, Emma Thomson, Karsten Thierbach,
Matthias Thoms and Ed Hurt:
Probing assembly of macromolecular protein complexes by a non-radioactive translation-controlled pulse-chase method
.Mol. Cell 47, 788-796 (2012).

Stefan Amlacher, Phillip Sarges, Dirk Flemming, Vera van Noort, Ruth Kunze, Damien Devos, Manimozhiyan Arumugam, Peer Bork and Ed Hurt:
Insight into structure and assembly of the nuclear pore complex by utilizing the genome
of a eukaryotic thermophile
.Cell 146, 277-289 (2011).

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Philipp Stelter, Ruth Kunze, Jessica Fischer and Ed Hurt:
Probing the FG repeat network of nucleoporins defines structural and functional features of
the nuclear pore complex
.J. Cell Biol. 195, 183-192 (2011).

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Dirk Flemming, Karsten Thierbach, Philipp Stelter, Bettina Boettcher and Ed Hurt:
Precise mapping of subunits in multiprotein complexes by a versatile EM-label
.Nature Struct. Biol. 17, 775-778 (2010).

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Dirk Flemming, Philipp Sarges, Philipp Stelter, Andrea Hellwig,
Bettina Boettcher and Ed Hurt:
Two structurally distinct domains of the nucleoporin Nup170
cooperate to tether a subset of nucleoporins to nuclear pores
.J. Cell Biol.185, 387-395 (2009).

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Nils Schrader, Philipp Stelter, Dirk Flemming, Ruth Kunze, Ed Hurt* and Ingrid Vetter*
(*corresponding authors):
Structural basis of the Nic96 subcomplex organization in the
nuclear pore channel
.Mol. Cell 29, 46-55 (2008).

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Philipp Stelter, Ruth Kunze, Dirk Flemming, Dominic Höpfner, Meikel Diepholz, Peter
Philipsen, Bettina Böttcher and Ed Hurt:
Molecular basis for the functional interaction
of dynein light chain with the nuclear pore complex
.Nature Cell Biology 9, 788-769 (2007).

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Malik Lutzmann, Ruth Kunze, Andrea Buerer, Ueli Aebi and Ed Hurt: Modular Self-Assembly
of a Y-Shaped Multiprotein Complex from Seven Nucleoporins. -
.EMBO J. 21, 387-397 (2002).