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
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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