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PMID: 11024021 Published · ppublish English Journal Article

Identification of two novel RanGTP-binding proteins belonging to the importin beta superfamily.

The Journal of biological chemistry ·Vol. 275 ·No. 51 ·2000-12-22 ·Pages 40163-8

Kutay U, Hartmann E, Treichel N, Calado A, Carmo-Fonseca M, Prehn S, Kraft R, Gorlich D, Bischoff FR

Abstract

Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin beta superfamily of nuclear transport receptors. These transport receptors all directly interact with RanGTP to modulate the compartment-specific binding of their transport substrates. To identify new members of the importin beta family, we used affinity chromatography on immobilized RanGTP and isolated Ran-binding protein (RanBP) 16 from HeLa cell extracts. RanBP16 and its close human homologue, RanBP17, are distant members of the importin beta family. Like the other members of the transport receptor superfamily, RanBP16 interacts with the nuclear pore complex and is able to enter the nucleus independent of energy and additional nuclear transport receptors.

MeSH Terms
Amino Acid Sequence Animals Base Sequence DNA Primers HeLa Cells Humans Karyopherins Molecular Sequence Data Nuclear Proteins/metabolism Sequence Homology, Amino Acid ran GTP-Binding Protein/chemistry,metabolism
Chemicals
DNA Primers Karyopherins Nuclear Proteins ran GTP-Binding Protein
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Kutay U
Swiss Federal Institute of Technology Zürich, Institute of Biochemistry, 8092 Zürich, Switzerland. ulrike.kutay@bc.biol.ethz.ch
Hartmann E
Treichel N
Calado A
Carmo-Fonseca M
Prehn S
Kraft R
Gorlich D
Bischoff F R
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2000-12-22
Pages
40163-8
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Databases
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AF064729, AF222747
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