Recent insight into the role of FBXW7 as a tumor suppressor

Kanae Yumimoto; Keiichi I. Nakayama

doi:10.1016/j.semcancer.2020.02.017

Recent insight into the role of FBXW7 as a tumor suppressor

Kanae Yumimoto, Keiichi I. Nakayama

Department of Molecular and Cellular Biology

Research output: Contribution to journal › Review article › peer-review

56 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	1-15
Number of pages	15
Journal	Seminars in Cancer Biology
Volume	67
DOIs	https://doi.org/10.1016/j.semcancer.2020.02.017
Publication status	Published - Dec 2020

All Science Journal Classification (ASJC) codes

Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.semcancer.2020.02.017

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title = "Recent insight into the role of FBXW7 as a tumor suppressor",

abstract = "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.",

author = "Kanae Yumimoto and Nakayama, {Keiichi I.}",

note = "Funding Information: This work was supported in part by Japan Society for the Promotion of Science KAKENHI grants 17K07171 and 18H05037 , Japan Agency for Medical Research and Development (AMED) P-CREATE grant 19cm0106105h0004 , and the NAITO foundation . ",

year = "2020",

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doi = "10.1016/j.semcancer.2020.02.017",

language = "English",

volume = "67",

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journal = "Seminars in Cancer Biology",

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T1 - Recent insight into the role of FBXW7 as a tumor suppressor

AU - Yumimoto, Kanae

AU - Nakayama, Keiichi I.

N1 - Funding Information: This work was supported in part by Japan Society for the Promotion of Science KAKENHI grants 17K07171 and 18H05037 , Japan Agency for Medical Research and Development (AMED) P-CREATE grant 19cm0106105h0004 , and the NAITO foundation .

PY - 2020/12

Y1 - 2020/12

N2 - 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.

AB - 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.

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DO - 10.1016/j.semcancer.2020.02.017

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SP - 1

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JO - Seminars in Cancer Biology

JF - Seminars in Cancer Biology

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Recent insight into the role of FBXW7 as a tumor suppressor

Abstract

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