A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export.
نویسندگان
چکیده
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 criteria, Yrb2p interacts with Xpo1p and not with other members of the importin/karyopherin beta superfamily. Moreover, the Yrb2p region containing nucleoporin-like FG repeats is important for NES-mediated protein export. Taken together, these data suggest that Yrb2p acts inside the nucleus to mediate the action of Xpo1p in at least one of several nuclear export pathways.
منابع مشابه
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 کاملStructural insights into how Yrb2p accelerates the assembly of the Xpo1p nuclear export complex.
Proteins and ribonucleoproteins containing a nuclear export signal (NES) assemble with the exportin Xpo1p (yeast CRM1) and Gsp1p-GTP (yeast Ran-GTP) in the nucleus and exit through the nuclear pore complex. In the cytoplasm, Yrb1p (yeast RanBP1) displaces NES from Xpo1p. Efficient export of NES-cargoes requires Yrb2p (yeast RanBP3), a primarily nuclear protein containing nucleoporin-like phenyl...
متن کاملThe nuclear export receptor Xpo1p forms distinct complexes with NES transport substrates and the yeast Ran binding protein 1 (Yrb1p).
Xpo1p (Crm1p) is the nuclear export receptor for proteins containing a leucine-rich nuclear export signal (NES). Xpo1p, the NES-containing protein, and GTP-bound Ran form a complex in the nucleus that translocates across the nuclear pore. We have identified Yrb1p as the major Xpo1p-binding protein in Saccharomyces cerevisiae extracts in the presence of GTP-bound Gsp1p (yeast Ran). Yrb1p is cyto...
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BACKGROUND Transport of macromolecules between the nucleus and cytoplasm of eukaryotic cells is mediated by nuclear import and export receptors. The receptors identified to date are members of a family of Ran GTPase-binding proteins whose founding member is importin-beta. Interaction between these receptors and their cargo is regulated by the GTP-bound form of Ran. Export complexes form and imp...
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Ran is the only known member of the Ras superfamily of small GTP-binding proteins to be localized primarily inside the nucleus, and there is considerable evidence that Ran is closely involved in the traffic of macromolecules into and out of the nucleus [1,2]. Ran has been shown to be an essential factor for nuclear import in digitonin-permeabilized cells, and mutant forms of Ran inhibit both pr...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 95 13 شماره
صفحات -
تاریخ انتشار 1998