Fornerod M, Ohno M, Yoshida M, Mattaj I W
European Molecular Biology Laboratory, Heidelberg, Germany.
Cell. 1997 Sep 19;90(6):1051-60. doi: 10.1016/s0092-8674(00)80371-2.
CRM1 is distantly related to receptors that mediate nuclear protein import and was previously shown to interact with the nuclear pore complex. Overexpression of CRM1 in Xenopus oocytes stimulates Rev and U snRNA export from the nucleus. Conversely, leptomycin B, a cytotoxin that is shown to bind to CRM1 protein, specifically inhibits the nuclear export of Rev and U snRNAs. In vitro, CRM1 forms a leptomycin B-sensitive complex involving cooperative binding of both RanGTP and the nuclear export signal (NES) from either the Rev or PKI proteins. We conclude that CRM1 is an export receptor for leucine-rich nuclear export signals and discuss a model for the role of RanGTP in CRM1 function and in nuclear export in general.
CRM1与介导核蛋白输入的受体有较远的亲缘关系，先前已证明它能与核孔复合体相互作用。在非洲爪蟾卵母细胞中过表达CRM1会刺激Rev和U snRNA从细胞核输出。相反，已证明与CRM1蛋白结合的细胞毒素莱普霉素B能特异性抑制Rev和U snRNA的核输出。在体外，CRM1形成一种对莱普霉素B敏感的复合体，该复合体涉及RanGTP与Rev或PKI蛋白的核输出信号（NES）的协同结合。我们得出结论，CRM1是富含亮氨酸的核输出信号的输出受体，并讨论了RanGTP在CRM1功能及一般核输出中作用的模型。
