Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka, 812-8582, Japan.
Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka, 812-8582, Japan.
Semin Cancer Biol. 2020 Dec;67(Pt 2):1-15. doi: 10.1016/j.semcancer.2020.02.017. Epub 2020 Feb 27.
FBXW7 (also known as Fbw7, Sel10, hCDC4, or hAgo) is a tumor suppressor and the most frequently mutated member of the F-box protein family in human cancers. FBXW7 functions as the substrate recognition component of an SCF-type E3 ubiquitin ligase. It specifically controls the proteasome-mediated degradation of many oncoproteins such as c-MYC, NOTCH, KLF5, cyclin E, c-JUN, and MCL1. In this review, we summarize the molecular and biological features of FBXW7 and its substrates as well as the impact of mutations of FBXW7 on cancer development. We also address the clinical potential of anticancer therapy targeting FBXW7.
FBXW7（也称为 Fbw7、Sel10、hCDC4 或 hAgo）是一种肿瘤抑制因子，也是人类癌症中 F-box 蛋白家族中最常发生突变的成员。FBXW7 作为一种 SCF 型 E3 泛素连接酶的底物识别组件发挥作用。它特异性地控制许多癌蛋白的蛋白酶体介导的降解，如 c-MYC、NOTCH、KLF5、cyclin E、c-JUN 和 MCL1。在这篇综述中，我们总结了 FBXW7 及其底物的分子和生物学特征，以及 FBXW7 突变对癌症发展的影响。我们还探讨了针对 FBXW7 的抗癌治疗的临床潜力。
