Ran-Binding Protein 3 Is a Cofactor for Crm1-Mediated Nuclear Protein Export
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Ran-Binding Protein 3 Is a Cofactor for Crm1-Mediated Nuclear Protein Export
Crm1 is a member of the karyopherin family of nucleocytoplasmic transport receptors and mediates the export of proteins from the nucleus by forming a ternary complex with cargo and Ran:GTP. This complex translocates through the nuclear pores and dissociates in the cytosol. The yeast protein Yrb2p participates in this pathway and binds Crm1, but its mechanism of action has not been established. ...
متن کاملA member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.
Yeast cells mutated in YRB2, which encodes a nuclear protein with similarity to other Ran-binding proteins, fail to export nuclear export signal (NES)-containing proteins including HIV Rev out of the nucleus. Unlike Xpo1p/Crm1p/exportin, an NES receptor, Yrb2p does not shuttle between the nucleus and the cytoplasm but instead remains inside the nucleus. However, by both biochemical and genetic ...
متن کاملA nuclear export signal is essential for the cytosolic localization of the Ran binding protein, RanBP1
RanBP1 is a Ran/TC4 binding protein that can promote the interaction between Ran and beta-importin /beta-karyopherin, a component of the docking complex for nuclear protein cargo. This interaction occurs through a Ran binding domain (RBD). Here we show that RanBP1 is primarily cytoplasmic, but the isolated RBD accumulates in the nucleus. A region COOH-terminal to the RBD is responsible for this...
متن کاملThe Mobile FG Nucleoporin Nup98 Is a Cofactor for Crm1-dependent Protein Export
Nup98 is a mobile nucleoporin that forms distinct dots in the nucleus, and, although a role for Nup98 in nuclear transport has been suggested, its precise function remains unclear. Here, we show that Nup98 plays an important role in Crm1-mediated nuclear protein export. Nuclear, but not cytoplasmic, dots of EGFP-tagged Nup98 disappeared rapidly after cell treatment with leptomycin B, a specific...
متن کاملCRM1- and Ran-independent nuclear export of β-catenin
Background: Activation of the Wnt pathway induces -catenin to localize Address: Max-Planck-Institute for Developmental Biology, Department of Cell Biology, Tübingen inside the nucleus, where it interacts with transcription factors such as D-72076, Germany. TCF/LEF-1. Regulation of the pathway occurs through a -catenin– degrading complex based on Axin and the tumor suppressor APC. We have Corres...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2001
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.153.7.1391