TY - JOUR
T1 - Identification of two novel RanGTP-binding proteins belonging to the importin β superfamily
AU - Kutay, Ulrike
AU - Hartmann, Enno
AU - Treichel, Nathalie
AU - Calado, Angelo
AU - Carmo-Fonseca, Maria
AU - Prehn, Siegfried
AU - Kraft, Regine
AU - Görlich, Dirk
AU - Bischoff, F. Ralf
PY - 2000/12/22
Y1 - 2000/12/22
N2 - Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin β 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 β 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 β 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.
AB - Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin β 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 β 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 β 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.
UR - http://www.scopus.com/inward/record.url?scp=0034704091&partnerID=8YFLogxK
U2 - 10.1074/jbc.M006242200
DO - 10.1074/jbc.M006242200
M3 - Journal articles
C2 - 11024021
AN - SCOPUS:0034704091
SN - 0021-9258
VL - 275
SP - 40163
EP - 40168
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 51
ER -