Dipartimento di Ematologia e Scienze Oncologiche Lorenzo e Ariosto Seràgnoli, University of Bologna, Italy.
Leuk Res. 2010 May;34(5):641-8. doi: 10.1016/j.leukres.2009.07.012. Epub 2009 Jul 29.
Constitutive tyrosine kinase (TK) activity of p210 BCR-ABL fusion protein of chronic myeloid leukemia (CML) usurps physiological functions of normal p145 c-ABL protein. Accordingly, its inhibition by imatinib mesylate (IM) lets p145 c-ABL translocate into the nuclear compartment, which drives cell growth arrest and apoptotic death. Here we show that IM and the mammalian target of rapamycin (mTOR) inhibitor RAD001 (Everolimus) have additive effects on BCR-ABL-expressing cells. Those effects are at least partly conditional upon the enhanced nuclear accumulation of p145 c-ABL through events encompassing post-translational modifications of p145 c-ABL (Thr(735) phosphorylation) precluding its nuclear export and of 14-3-3 sigma (Ser(186) phosphorylation by c-Jun N-terminal kinase [JNK]) promoting p145 c-ABL nuclear re-import.
慢性髓性白血病(CML)中 p210 BCR-ABL 融合蛋白的组成型酪氨酸激酶(TK)活性篡夺了正常 p145 c-ABL 蛋白的生理功能。因此,其被甲磺酸伊马替尼(IM)抑制会导致 p145 c-ABL 转位到核区,从而驱动细胞生长停滞和凋亡。在这里,我们表明 IM 和雷帕霉素(mTOR)抑制剂 RAD001(依维莫司)对表达 BCR-ABL 的细胞具有相加作用。这些作用至少部分取决于通过事件增强 p145 c-ABL 的核积累,这些事件包括 p145 c-ABL 的翻译后修饰(Thr(735)磷酸化),阻止其核输出和 14-3-3 sigma(c-Jun N-末端激酶[JNK]介导的 Ser(186)磷酸化)促进 p145 c-ABL 核再导入。