USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication
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- 作者：Santiago Herná ; ndez-Pé ; reza ; 1 ; Elisa Cabreraa ; 1 ; Hugo Amoedoa ; 1 ; 2 ; Sara Rodrí ; guez-Acebesb ; Stephane Koundrioukoffc ; d ; e ; Michelle Debatissec ; d ; e ; Juan Mé ; ndezb ; Raimundo Freirea ; rfreire@ull.edu.es" class="auth_mail" title="E-mail the corresponding author
- 关键词：Initiation of DNA replication ; DNA damage response ; Ubiquitin hydrolase ; DNA damage ; Protein degradation ; Proteasome
- 刊名：Molecular Oncology
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：10
- 期：8
- 页码：1196-1206
- 全文大小：1543 K
文摘
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We identified a ubiquitin hydrolase that controls the DNA replication licensing protein Cdt1: USP37.
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USP37 stabilizes mainly a low mobility form of Cdt1 that is unstable and likely to be phosphorylated.
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USP37 and Cdt1 interact and USP37 is able to de-ubiquitinate Cdt1 in vivo.
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USP37 overexpression increases the MCM7 loading on the chromatin.
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USP37 downregulation decreases replication fork speed, indicating a function in DNA replication.