The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

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• 作者：Qi Zhang^a ; Zhongduo Wang^b ; Feng Hou^a ; Rachel Harding^a ; Xinyi Huang^c ; Aiping Dong^a ; John R. Walker^a ; Yufeng Tong^a ; ^c ; ^{yufeng.tong@utoronto.ca}
• 关键词：DUB ; Deubiquitinase ; ERAD ; endoplasmic-reticulum associated degradation ; ESI ; electrospray ionization ; HEPES ; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid ; ITC ; isothermal titration calorimetry ; ML ; maximum-likelihood ; RING ; really-interesting new genes ; SBD ; substrate binding domain ; SIAH ; seven in absentia homolog ; Tagg ; temperature of aggregation ; TCEP ; tris(2-carboxyethyl)phosphine ; TEV ; tobacco etch virus ; USP ; ubiquitin-specific protease ; ZnF ; zinc finger
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3095-3105
• 全文大小：1833 K
• 卷排序：1861

文摘

Crystal structures of apo-SIAH2 and USP19/SIAH1 complex are solved. USP19 is the only deubiquitinase found to bind with SIAH E3 ubiquitin ligases. The USP19/SIAH complex is conserved in evolution. Menadione destabilizes both SIAH1 and SIAH2 non-specifically.