The Human Homologue of Yeast CRM1 is in a Dynamic Subcomplex with CAN/Nup214 and a Novel Nuclear Pore Component Nup88
Autor: | Gerard Grosveld, K. Gopal Murti, Sjozef van Baal, Maarten Fornerod, Albert B. Reynolds, Donna S. Davis, Jack Fransen, Jan M. van Deursen |
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Jazyk: | angličtina |
Rok vydání: | 1997 |
Předmět: |
Nuclear Envelope
Molecular Sequence Data Receptors Cytoplasmic and Nuclear Saccharomyces cerevisiae Biology Karyopherins General Biochemistry Genetics and Molecular Biology Cell Line Fungal Proteins Mice Exportin-1 RNA Polymerase I Intracellulair transport van glycoprotëinen in gepolariseerde epitheelcellen epitheelcellen medicine Animals Humans Amino Acid Sequence Nuclear protein Nuclear pore Cloning Molecular GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) Molecular Biology Cell Nucleus Nucleoplasm General Immunology and Microbiology Base Sequence Sequence Homology Amino Acid General Neuroscience Nucleocytoplasmic Transport Proteins fungi food and beverages Membrane Proteins Nuclear Proteins Sequence Analysis DNA beta Karyopherins Molecular Weight Nuclear Pore Complex Proteins Cell nucleus stomatognathic diseases medicine.anatomical_structure Blastocyst Biochemistry Dactinomycin Nucleoporin Nuclear transport Intracellular transport of glycoproteins in polarized epithelial cells Carrier Proteins Research Article Protein Binding |
Zdroj: | EMBO Journal, 16, 4, pp. 807-816 EMBO Journal, 16, 807-816 |
ISSN: | 0261-4189 |
Popis: | The oncogenic nucleoporin CAN/Nup214 is essential in vertebrate cells. Its depletion results in defective nuclear protein import, inhibition of messenger RNA export and cell cycle arrest. We recently found that CAN associates with proteins of 88 and 112 kDa, which we have now cloned and characterized. The 88 kDa protein is a novel nuclear pore complex (NPC) component, which we have named Nup88. Depletion of CAN from the NPC results in concomitant loss of Nup88, indicating that the localization of Nup88 to the NPC is dependent on CAN binding. The 112 kDa protein is the human homologue of yeast CRM1, a protein known to be required for maintenance of correct chromosome structure. This human CRM1 (hCRM1) localized to the NPC as well as to the nucleoplasm. Nuclear overexpression of the FG-repeat region of CAN, containing its hCRM1-interaction domain, resulted in depletion of hCRM1 from the NPC. In CAN-/- mouse embryos lacking CAN, hCRM1 remained in the nuclear envelope, suggesting that this protein can also bind to other repeat-containing nucleoporins. Lastly, hCRM1 shares a domain of significant homology with importin-beta, a cytoplasmic transport factor that interacts with nucleoporin repeat regions. We propose that hCRM1 is a soluble nuclear transport factor that interacts with the NPC. |
Databáze: | OpenAIRE |
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