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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Visser, G. D. Adam, S. A. Chi, N. C. Adam, E. J. |
| Description | Author Affiliation: Chi NC ( Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA.) |
| Abstract | Three factors have been identified that reconstitute nuclear protein import in a permeabilized cell assay: the NLS receptor, p97, and Ran/TC4. Ran/TC4, in turn, interacts with a number of proteins that are involved in the regulation of GTP hydrolysis or are components of the nuclear pore. Two Ran-binding proteins, RanBP1 and RanBP2, form discrete complexes with p97 as demonstrated by immunoadsorption from HeLa cell extracts fractionated by gel filtration chromatography. A > 400-kD complex contains p97, Ran, and RanBP2. Another complex of 150- 300 kD was comprised of p97, Ran, and RanBP1. This second trimeric complex could be reconstituted from recombinant proteins. In solution binding assays, Ran-GTP bound p97 with high affinity, but the binding of Ran-GDP to p97 was undetectable. The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Binding of Ran-GTP to p97 dissociated p97 from immobilized NLS receptor while the Ran-GDP/RanBP1/p97 complex did not dissociate from the receptor. In a digitonin-permeabilized cell docking assay, RanBP1 stabilizes the receptor complex against temperature-dependent release from the pore. When added to an import assay with recombinant NLS receptor, p97 and Ran-GDP, RanBP1 significantly stimulates transport. These results suggest that RanBP1 promotes both the docking and translocation steps in nuclear protein import by stabilizing the interaction of Ran-GDP with p97. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 3 |
| Volume Number | 135 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1996-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | GTP-Binding Proteins Metabolism Nuclear Pore Complex Proteins Nuclear Proteins Biological Transport Cell Membrane Permeability Drug Effects Cell Nucleus DNA-Binding Proteins Digitonin Pharmacology Guanosine Diphosphate Guanosine Triphosphate HeLa Cells Macromolecular Substances Molecular Chaperones Nuclear Envelope Chemistry Protein Binding Recombinant Fusion Proteins Isolation & Purification Alpha Karyopherins Beta Karyopherins Ran GTP-Binding Protein Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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