Ubc9 fusion-directed SUMOylation (UFDS)

被引:9
|
作者
Niedenthal, R. [1 ]
机构
[1] Hannover Med Sch, Inst Physiol Chem, D-30625 Hannover, Germany
关键词
E2 conjugating enzyme; protein modification; signal transducer and activator of transcription 1 (STAT1); small ubiquitin-related modifier (SUMO); SUMOylation-regulated phosphorylation; Ubc9 fusion-directed SUMOylation (UFDS); ubiquitin-conjugating enzyme 9 (Ubc9);
D O I
10.1042/BST0351430
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
SUMOylation is a post-translational modification that is involved in the regulation of proteins of different cellular processes. Dependent on the transient, small SUMOylated portion of most target proteins, it is difficult to identify and characterize this modification and its functions, and it is even more difficult to study the interplay between SUMOylation and other modifications on a specific protein. To facilitate the analysis of protein SUMOylation and its interplay with other protein modifications, the UFDS (ubc9 fusion-directed SUMOylation) system has been developed. The identification of new SUMOylation substrates and the elucidation of the interplay between STAT1 (signal transducer and activator of transcription 1) phosphorylation and SUMOylation demonstrate UFDS as a useful tool for analysing protein SUMOylation.
引用
收藏
页码:1430 / 1432
页数:3
相关论文
共 50 条
  • [21] A role for Ubc9 in tumorigenesis
    Mo, YY
    Yu, YN
    Theodosiou, E
    Ee, PLR
    Beck, WT
    ONCOGENE, 2005, 24 (16) : 2677 - 2683
  • [22] A role for Ubc9 in tumorigenesis
    Yin-Yuan Mo
    Yanni Yu
    Elena Theodosiou
    P L Rachel Ee
    William T Beck
    Oncogene, 2005, 24 : 2677 - 2683
  • [23] Sumoylation by Ubc9 Regulates the Stem Cell Compartment and Structure and Function of the Intestinal Epithelium in Mice
    Demarque, Maud D.
    Nacerddine, Karim
    Neyret-Kahn, Helene
    Andrieux, Alexandra
    Danenberg, Esther
    Jouvion, Gregory
    Bomme, Perrine
    Hamard, Ghislaine
    Romagnolo, Beatrice
    Terris, Benoit
    Cumano, Ana
    Barker, Nick
    Clevers, Hans
    Dejean, Anne
    GASTROENTEROLOGY, 2011, 140 (01) : 286 - 296
  • [24] Modulation of PLAGL2 transactivation activity by Ubc9 co-activation not SUMOylation
    Guo, Yuhong
    Yang, Meng-Chun W.
    Weissler, Jonathan C.
    Yang, Yih-Sheng
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2008, 374 (03) : 570 - 575
  • [25] Nuclear accumulation of UBC9 contributes to SUMOylation of lamin A/C and nucleophagy in response to DNA damage
    Li, Yunong
    Jiang, Xiuxing
    Zhang, Yanhao
    Gao, Ziyi
    Liu, Yanxia
    Hu, Jinjiao
    Hu, Xiaoye
    Li, Lirong
    Shi, Jingshan
    Gao, Ning
    JOURNAL OF EXPERIMENTAL & CLINICAL CANCER RESEARCH, 2019, 38 (1)
  • [26] Nuclear accumulation of UBC9 contributes to SUMOylation of lamin A/C and nucleophagy in response to DNA damage
    Yunong Li
    Xiuxing Jiang
    Yanhao Zhang
    Ziyi Gao
    Yanxia Liu
    Jinjiao Hu
    Xiaoye Hu
    Lirong Li
    Jingshan Shi
    Ning Gao
    Journal of Experimental & Clinical Cancer Research, 38
  • [27] Targeting Ubc9 for cancer therapy
    Mo, YY
    Moschos, SJ
    EXPERT OPINION ON THERAPEUTIC TARGETS, 2005, 9 (06) : 1203 - 1216
  • [28] RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation
    Yan, Jun
    Yang, Xiao-Ping
    Kim, Yong-Sik
    Joo, Joung Hyuck
    Jetten, Anton M.
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 362 (01) : 132 - 138
  • [29] The breast cancer associated gene 2 (BCA2) binds to Ubc9 and is involved in sumoylation
    Kona, Fathima R.
    Stark, Karri
    Bisosk, Luke
    Zhang, Xiang-Dong
    Seth, Arun
    Burgers, Angelika
    CANCER RESEARCH, 2011, 71
  • [30] Manipulating PML SUMOylation via Silencing UBC9 and RNF4 Regulates Cardiac Fibrosis
    Liu, Yu
    Zhao, Dan
    Qiu, Fang
    Zhang, Ling-Ling
    Liu, Shang-Kun
    Li, Yuan-Yuan
    Liu, Mei-Tong
    Wu, Di
    Wang, Jia-Xin
    Ding, Xiao-Qing
    Liu, Yan-Xin
    Dong, Chang-Jiang
    Shao, Xiao-Qi
    Yang, Bao-Feng
    Chu, Wen-Feng
    MOLECULAR THERAPY, 2017, 25 (03) : 666 - 678