Influence of cargo size on Ran and energy requirements for nuclear protein import
Autor: | Janna Bednenko, Larry Gerace, Harald Wodrich, Tinglu Guan, Susan K. Lyman |
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Rok vydání: | 2002 |
Předmět: |
alpha Karyopherins
GTP' Recombinant Fusion Proteins Active Transport Cell Nucleus Importin Guanosine triphosphate Biology Article 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Humans Nuclear pore nuclear protein import importin β transportin nucleoporin Ran 030304 developmental biology Cell Nucleus 0303 health sciences Binding Sites Alpha Karyopherins Cell Biology beta Karyopherins Protein Structure Tertiary Cell biology Molecular Weight ran GTP-Binding Protein chemistry Karyopherins Nuclear Pore Beta Karyopherins Guanosine Triphosphate 030217 neurology & neurosurgery HeLa Cells |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.200204163 |
Popis: | Previous work has shown that the transport of some small protein cargoes through the nuclear pore complex (NPC) can occur in vitro in the absence of nucleoside triphosphate hydrolysis. We now demonstrate that in the importin α/β and transportin import pathways, efficient in vitro transport of large proteins, in contrast to smaller proteins, requires hydrolyzable GTP and the small GTPase Ran. Morphological and biochemical analysis indicates that the presence of Ran and GTP allows large cargo to efficiently cross central regions of the NPC. We further demonstrate that this function of RanGTP at least partly involves its direct binding to importin β and transportin. We suggest that RanGTP functions in these pathways to promote the transport of large cargo by enhancing the ability of import complexes to traverse diffusionally restricted areas of the NPC. |
Databáze: | OpenAIRE |
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