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鉴定导致 FAM122A 的 SUMO1 修饰物被泛素-蛋白酶体系统降解的 PP2A-Cα。

Identifying the SUMO1 modification of FAM122A leading to the degradation of PP2A-Cα by ubiquitin-proteasome system.

机构信息

Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.

Department of Pathophysiology, Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Rui-jin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.

出版信息

Biochem Biophys Res Commun. 2018 Jun 7;500(3):676-681. doi: 10.1016/j.bbrc.2018.04.135. Epub 2018 Apr 22.

DOI:10.1016/j.bbrc.2018.04.135
PMID:29678583
Abstract

FAM122A is a highly conserved protein in mammals. Here, we identify that FAM122A can be sumoylated at lysine 89, which can be de-conjugated by SENP1. Furthermore, the sumoylation of FAM122A reduces the PP2A-Cα protein level together with the reduced phosphatase activity of PP2A, which suppresses cell proliferation. Collectively, our results suggest that the sumoylation of FAM122A may have a significant role in cellular function.

摘要

FAM122A 是哺乳动物中高度保守的蛋白。在这里,我们鉴定出 FAM122A 可以赖氨酸 89 位发生 SUMO 化修饰,该修饰可以被 SENP1 酶切除。此外,FAM122A 的 SUMO 化修饰会降低 PP2A-Cα 蛋白水平,同时降低 PP2A 的磷酸酶活性,从而抑制细胞增殖。综上,我们的研究结果提示 FAM122A 的 SUMO 化修饰可能在细胞功能中发挥重要作用。

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Biochem Biophys Res Commun. 2018 Jun 7;500(3):676-681. doi: 10.1016/j.bbrc.2018.04.135. Epub 2018 Apr 22.
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FAM122A ensures cell cycle interphase progression and checkpoint control by inhibiting B55α/PP2A through helical motifs.FAM122A 通过螺旋结构域抑制 B55α/PP2A,从而确保细胞周期间期中的进展和检查点控制。
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