Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes

Autor: Petra Schwarzmaier, Gerd Lipowsky, Enno Hartmann, Susanne Kostka, Regine Kraft, Ulrike Kutay, F. Ralf Bischoff, Dirk Görlich
Rok vydání: 2000
Předmět:
Cytoplasm
DNA
Complementary
Time Factors
Molecular Sequence Data
Importin
Karyopherins
Biology
environment and public health
Chromatography
Affinity
General Biochemistry
Genetics and Molecular Biology
GTP Phosphohydrolases
Mice
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Peptide Initiation Factors
Animals
Humans
Amino Acid Sequence
Cloning
Molecular
Nuclear pore
Nuclear protein
Nuclear export signal
Molecular Biology
030304 developmental biology
Cell Nucleus
Hypusine
0303 health sciences
Dose-Response Relationship
Drug
General Immunology and Microbiology
Lysine
General Neuroscience
Nuclear Proteins
RNA-Binding Proteins
Articles
Protein Structure
Tertiary
Kinetics
ran GTP-Binding Protein
Microscopy
Fluorescence
Biochemistry
chemistry
030220 oncology & carcinogenesis
Ran
RNA
Nucleoporin
Nuclear transport
Carrier Proteins
HeLa Cells
Protein Binding
Zdroj: The EMBO Journal
Scopus-Elsevier
ISSN: 1460-2075
DOI: 10.1093/emboj/19.16.4362
Popis: Transport receptors of the importin beta superfamily account for many of the nuclear import and export events in eukaryotic cells. They mediate translocation through nuclear pore complexes, shuttle between nucleus and cytoplasm and co-operate with the RanGTPase system to regulate their interactions with cargo molecules in a compartment-specific manner. We used affinity chromatography on immobilized RanGTP to isolate further candidate nuclear transport receptors and thereby identified exportin 4 as the most distant member of the importin beta family so far. Exportin 4 appears to be conserved amongst higher eukaryotes, but lacks obvious orthologues in yeast. It mediates nuclear export of eIF-5A (eukaryotic translation initiation factor 5A) and possibly that of other cargoes. The export signal in eIF-5A appears to be complex and to involve the hypusine modification that is unique to eIF-5A. We discuss possible cellular roles for nuclear export of eIF-5A.
Databáze: OpenAIRE
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