Identifying the SUMO1 modification of FAM122A leading to the degradation of PP2A-C&#945; by ubiquitin-proteasome system.

Fan, Fangzhi; Zhao, Junxing; Liu, Yali; Zhao, Hongfang; Weng, Lietao; Li, Qingqing; Chen, Guoqiang; Xu, Ying

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

Fan, Fangzhi; Zhao, Junxing; Liu, Yali; Zhao, Hongfang; Weng, Lietao; Li, Qingqing; Chen, Guoqiang; Xu, Ying.

Afiliação

Fan F; 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.
Zhao J; 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.
Liu Y; Institute of Health Sciences, Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences and SJTU-SM, Shanghai 200025, China.
Zhao H; Institute of Health Sciences, Shanghai Institutes for Biological Sciences of Chinese Academy of Sciences and SJTU-SM, Shanghai 200025, China.
Weng L; 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.
Li Q; 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.
Chen G; 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 E
Xu Y; 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. Electronic address: yingxuxu@shsmu.edu.cn.

Biochem Biophys Res Commun ; 500(3): 676-681, 2018 06 07.

Article em En | MEDLINE | ID: mdl-29678583

ABSTRACT

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.

Assuntos

Fosfoproteínas/metabolismo; Complexo de Endopeptidases do Proteassoma/metabolismo; Proteína Fosfatase 2/metabolismo; Processamento de Proteína Pós-Traducional; Proteólise; Proteína SUMO-1/metabolismo; Ubiquitina/metabolismo; Sequência de Aminoácidos; Proliferação de Células; Células HEK293; Humanos; Lisina/metabolismo; Fosfoproteínas/química; Sumoilação

Palavras-chave

FAM122A; PP2A; Phosphatase activity; SUMO1 modification; Ubiquitination

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfoproteínas / Processamento de Proteína Pós-Traducional / Proteína SUMO-1 / Ubiquitina / Complexo de Endopeptidases do Proteassoma / Proteína Fosfatase 2 / Proteólise Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2018 Tipo de documento: Article

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