Cole, C. N., Hammell, C. M. (1998) Nucleocytoplasmic transport: Driving and directing transport. Current Biology, 8 (11). R368-R372. ISSN 09609822 (ISSN)
Abstract
Nucleocytoplasmic transport involves assembly and movement across the nuclear envelope of cargo-receptor complexes that interact with the small GTPase Ran. The asymmetric distribution of Ran regulator proteins, RanGAP1 and RCC1, provides the driving force and directionality for nuclear transport.
Item Type: | Paper |
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Uncontrolled Keywords: | carrier protein cell cycle protein DNA binding protein guanine nucleotide exchange factor guanosine diphosphate guanosine triphosphatase guanosine triphosphatase activating protein guanosine triphosphate nuclear protein Ran protein RCC1 protein, human active transport animal article biological model cell nucleus cytoplasm metabolism Saccharomyces cerevisiae Animals Biological Transport, Active Carrier Proteins Cell Cycle Proteins DNA-Binding Proteins GTP Phosphohydrolases GTPase-Activating Proteins Guanine Nucleotide Exchange Factors Models, Biological Nuclear Proteins ran GTP-Binding Protein Animalia |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing bioinformatics > genomics and proteomics bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein organs, tissues, organelles, cell types and functions > organelles, types and functions > nucleus organs, tissues, organelles, cell types and functions > organelles, types and functions bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types |
CSHL Authors: | |
Communities: | CSHL labs > Hammell C. lab |
Depositing User: | Matt Covey |
Date: | 1998 |
Date Deposited: | 11 Mar 2013 16:58 |
Last Modified: | 11 Mar 2013 16:58 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/27742 |
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