期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 20, 期 12, 页码 4295-4308出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.20.12.4295-4308.2000
关键词
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The RanGTP-binding protein RanBP1, which is located in the cytoplasm, has been implicated in release of nuclear export complexes from the cytoplasmic side of the nuclear pore complex. Here we show that Yrb1 (the yeast homolog of RanBP1) shuttles between the nucleus and the cytoplasm. Nuclear import of Yrb1 is a facilitated process that requires a short basic sequence uithin the Ran-binding domain (RBD). By contrast, nuclear export of Yrb1 requires an intact RBD, which forms a ternary complex wvith the Xpo1 (Crm1) NES receptor in the presence of RanGTP. Nuclear export of Yrb1, however, is insensitive towards leptomycin B, suggesting a novel type of substrate recognition between Yrb1 and Xpo1. Taken together, these data suggest that ongoing nuclear impart and export is an important feature of Yrb1 function in vivo.
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