Research Topics
Genomes and Genes
| D GorlichSummaryAffiliation: University of Heidelberg Country: Germany Publications
| Collaborators
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Detail Information
Publications
Transport between the cell nucleus and the cytoplasmD Gorlich
Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany
Annu Rev Cell Dev Biol 15:607-60. 1999..We discuss mechanistic aspects and the energetics of transport receptor function and describe a number of pathways in detail...
Nuclear protein importD Gorlich
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany
Curr Opin Cell Biol 9:412-9. 1997..Although an understanding of some of the steps in the import process is emerging, the molecular mechanism of the actual translocation through the NPC is still obscure...
A novel class of RanGTP binding proteinsD Gorlich
Zentrum fur Molekulare Biologie der Universitat Heidelberg, 69120 Heidelberg, Germany
J Cell Biol 138:65-80. 1997..On the basis of these results, we propose that RanBP7 might represent a nuclear transport factor that carries an as yet unknown cargo, which could apply as well for this entire class of related RanGTP-binding proteins...
Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotesG Lipowsky
ZMBH, 69120 Heidelberg, Germany
EMBO J 19:4362-71. 2000..The export signal in eIF-5A appears to be complex and to involve the hypusine modification that is unique to eIF-5A. We discuss possible cellular roles for nuclear export of eIF-5A...
Identification of a tRNA-specific nuclear export receptorU Kutay
Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany
Mol Cell 1:359-69. 1998..RanGTP regulates the substrate-exportin-t interaction such that tRNA can be preferentially bound in the nucleus and released in the cytoplasm...
Export of importin alpha from the nucleus is mediated by a specific nuclear transport factorU Kutay
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Federal Republic of Germany
Cell 90:1061-71. 1997..Importin alpha is released from this complex in the cytoplasm by the combined action of RanBP1 and RanGAP1. CAS binds preferentially to NLS-free importin alpha, explaining why import substrates stay in the nucleus...
CRM1-mediated recycling of snurportin 1 to the cytoplasmE Paraskeva
Zentrum fur Molekulare Biologie der Universitat Heidelberg, D 69120 Heidelberg, Germany
J Cell Biol 145:255-64. 1999..This mechanism appears crucial for productive import cycles as it can ensure that CRM1 only exports snurportin 1 that has already released its import substrate in the nucleus...
The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substratesA Bachi
European Molecular Biology Laboratory, Heidelberg, Germany
RNA 6:136-58. 2000....
The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1S Jäkel
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Im Neuenheimer Feld 282, D 69120 Heidelberg, Germany
EMBO J 18:2411-23. 1999..Its Ran-binding site is essential when operating as an autonomous import receptor, i.e. independently of Impbeta. Within the Impbeta/Imp7 heterodimer, however, Imp7 plays a more passive role than Impbeta and resembles an import adapter...
Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cellsS Jäkel
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Germany
EMBO J 17:4491-502. 1998..The presence of distinct binding sites for rpL23a and the M9 import signal in transportin, and for rpL23a and importin alpha in importin beta might explain how a single receptor can recognize very different import signals...
NTF2 mediates nuclear import of RanK Ribbeck
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany
EMBO J 17:6587-98. 1998....
Identification of different roles for RanGDP and RanGTP in nuclear protein importD Gorlich
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Germany
EMBO J 15:5584-94. 1996..Thus, binding of nucleoplasmic RanGTP to importin-beta probably triggers termination, i.e. the dissociation of importin-alpha from importin-beta and the subsequent release of the import substrate into the nucleoplasm...
Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1R Deane
Abteilung Molekulare Biologie der Mitose, Deutsches Krebsforschungszentrum, Heidelberg, Germany
Mol Cell Biol 17:5087-96. 1997..We propose that RanBP5 is a mediator of a nucleocytoplasmic transport pathway that is distinct from the importin-alpha-dependent import of proteins with a classical NLS...
Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complexU Kutay
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Germany
EMBO J 16:1153-63. 1997..This suggests that mediators of these various transport events share binding sites on the NPC and/or that mechanisms exist to coordinate translocation through the NPC via different nucleocytoplasmic transport pathways...
RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factorsF R Bischoff
Abteilung Molekulare Biologie der Mitose, Deutsches Krebsforschungszentrum, Heidelberg, Germany
FEBS Lett 419:249-54. 1997..The transiently released RanGTP x RanBP1 complex is then induced by RanGAP to hydrolyse GTP, preventing the receptor to rebind RanGTP. The efficient release of importin beta from RanGTP requires importin alpha, in addition to RanBP1...
