An activity-based probe developed by a sequential dehydroalanine formation strategy targets HECT E3 ubiquitin ligases

被引：30

作者：

Xu, Ling ^{[1
]}

Fan, Jian ^{[1
]}

Wang, Yu ^{[2
]}

Zhang, Zhongping ^{[3
]}

Fu, Yao ^{[1
]}

Li, Yi-Ming ^{[2
]}

Shi, Jing ^{[1
]}

机构：

[1] Univ Sci & Technol China, Dept Chem, Hefei 230026, Anhui, Peoples R China

[2] Hefei Univ Technol, Sch Food & Biol Engn, Hefei 230009, Anhui, Peoples R China

[3] Chinese Acad Sci, Inst Intelligent Machines, Hefei 230031, Anhui, Peoples R China

来源：

CHEMICAL COMMUNICATIONS | 2019年 / 55卷 / 49期

基金：

国家重点研发计划; 中国国家自然科学基金;

关键词：

CHEMICAL-SYNTHESIS; PROTEINS; FAMILY; LIGATION; INSIGHTS; CYSTEINE; MEMBERS; CANCER; EDD;

D O I：

10.1039/c9cc03739j

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

E3 ligases play a critical role in ubiquitin (Ub) conjugation cascades, and any aberration in their activity is associated with a number of diseases. Advancement in our knowledge of understanding the roles of HECT E3s requires biochemical tools such as activity-based probes (ABPs). In this study we developed a novel dehydroalanine (Dha)-based E2-Ub ABP using a strategy that is a combination of practical hydrazide-based native chemical ligation and sequential Dha formation. The probe could be used for labeling HECT E3s not only in vitro but also in endogenous cellular contexts. Our easy-to-implement method is expected to be useful for the preparation of Dha based Ub family E2 conjugate ABPs.

引用

页码：7109 / 7112

页数：4

共 40 条

[31] Mechanism-Based Small Molecule Cross-Linkers of HECT E3 Ubiquitin Ligase-Substrate Pairs
Park, Sungjin
Ntai, Ioanna
Thomas, Paul
Konishcheva, Evgeniia
Kelleher, Neil L.
Statsuk, Alexander V.
BIOCHEMISTRY, 2012, 51 (42) : 8327 - 8329
[32] An Angelman syndrome substitution in the HECT E3 ubiquitin ligaseC-terminal Lobe of E6AP affects protein stability and activity
Beasley, Steven A.
Kellum, Chloe E.
Orlomoski, Rachel J.
Idrizi, Feston
Spratt, Donald E.
PLOS ONE, 2020, 15 (07):
[33] The Ubiquitin Conjugating Enzyme, UbcM2, Engages in Novel Interactions with Components of Cullin-3 Based E3 Ligases
Plafker, Kendra S.
Singer, Jeffrey D.
Plafker, Scott M.
BIOCHEMISTRY, 2009, 48 (15) : 3527 - 3537
[34] Haploid Genetic Screens Identify an Essential Role for PLP2 in the Downregulation of Novel Plasma Membrane Targets by Viral E3 Ubiquitin Ligases
Timms, Richard T.
Duncan, Lidia M.
Tchasovnikarova, Iva A.
Antrobus, Robin
Smith, Duncan L.
Dougan, Gordon
Weekes, Michael P.
Lehner, Paul J.
PLOS PATHOGENS, 2013, 9 (11):
[35] A cell-based high-throughput screening method based on a ubiquitin-reference technique for identifying modulators of E3 ligases
Tian, Maoyuan
Zeng, Taoling
Liu, Mingdong
Han, Shang
Lin, Huayue
Lin, Qi
Li, Li
Jiang, Tingting
Li, Gao
Lin, Hong
Zhang, Ting
Kang, Qiaofeng
Deng, Xianming
Wang, Hong-Rui
JOURNAL OF BIOLOGICAL CHEMISTRY, 2019, 294 (08) : 2880 - 2891
[36] Single-Domain Antibodies as Crystallization Chaperones to Enable Structure-Based Inhibitor Development for RBR E3 Ubiquitin Ligases
Tsai, Yi-Chun Isabella
Johansson, Henrik
Dixon, David
Martin, Stephen
Chung, Chun-wa
Clarkson, Jane
House, David
Rittinger, Katrin
CELL CHEMICAL BIOLOGY, 2020, 27 (01): : 83 - +
[37] Activity-based profiling of cullin-RING E3 networks by conformation-specific probes
Henneberg, Lukas T.
Singh, Jaspal
Duda, David M.
Baek, Kheewoong
Yanishevski, David
Murray, Peter J.
Mann, Matthias
Sidhu, Sachdev S.
Schulman, Brenda A.
NATURE CHEMICAL BIOLOGY, 2023, 19 (12) : 1513 - 1523
[38] Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases
Sarkar, Sayani
Behera, Adaitya Prasad
Borar, Prateeka
Banka, Prerana Agarwal
Datta, Ajit B.
BIOCHEMICAL JOURNAL, 2019, 476 : 1465 - 1482
[39] VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases
Nakagawa, Tadashi
Mondal, Koushik
Swanson, Patrick C.
BMC MOLECULAR BIOLOGY, 2013, 14
[40] Shigella IpaH0722 E3 Ubiquitin Ligase Effector Targets TRAF2 to Inhibit PKC-NF-κB Activity in Invaded Epithelial Cells
Ashida, Hiroshi
Nakano, Hiroyasu
Sasakawa, Chihiro
PLOS PATHOGENS, 2013, 9 (06)

← 1 2 3 4 →