Structures, functions, and assembly of the nuclear pore complexes
Project management at the University of Würzburg:
Nuclear pore complexes mediate the transmembrane exchange of macromolecules between the nucleus and the cytoplasm. These bidirectional transport processes are highly selective, saturable and energy-requiring. Knowledge of nuclear pore complex structure, composition and molecular organization is a necessary prerequisite to understanding these transport mechanisms. We are using both monoclonal antibodies against pore complex constituents and autoimmune antibodies from patient sera in order to identify novel members of the nucleoporins. Nuclear pore complexes are dynamic structures. During mitosis the nuclear envelope breaks down into numerous vesicles and reforms at telophase. In order to analyze the mode and order of interaction of the disassembled nuclear envelope and pore complex constituents during the reformation process, we have used a cell free extract. This extract is prepared from eggs of Xenopus laevis and capable of reproducing postmitotic reformation of the nuclear envelope and assembly of pore complexes.
nuclear pore complex
Xenopus egg extract
nuclear envelope assembly
from 01.1997 to 12.1999
DFG ( SFB 176 )
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(pp 475-478 (1994)). Nuclear pore complex structure analyzed by immunogold EM with human autoantibodies.. (monograph)
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- Wilken, N., J.L. Senécal, U. Scheer and M.C. Dabauvalle.
(68, 211-219 (1995)). Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. (monograph)
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(109, 1813-1824 (1996).). A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes.. (monograph)
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(73, 259-269 (1997)). Preassembly of annulate lamellae in egg extracts inhibits nuclear pore complex formation, but not nuclear membrane assembly.. (monograph)
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(80, 678-691 (2001)). Microtubule- dependent assembly of the nuclear envelope in Xenopus laevis egg extract. (monograph)