Ubiquitin ligases: structure, function, and regulation
N Zheng, N Shabek - Annual review of biochemistry, 2017 - annualreviews.org
Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …
ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …
[HTML][HTML] Structural mechanisms of HECT-type ubiquitin ligases
S Lorenz - Biological chemistry, 2018 - degruyter.com
Ubiquitin ligases (E3 enzymes) transfer ubiquitin from ubiquitin-conjugating (E2) enzymes to
target proteins. By determining the selection of target proteins, modification sites on those …
target proteins. By determining the selection of target proteins, modification sites on those …
[HTML][HTML] UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability
Nuclear hormone receptors (NRs) are ligand-binding transcription factors that are widely
targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation …
targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation …
[HTML][HTML] Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5
LA Hehl, D Horn-Ghetko, JR Prabu, R Vollrath… - Nature Chemical …, 2024 - nature.com
Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases
regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry …
regulates vast biology, yet the structural mechanisms remain unknown. We used chemistry …
Cryo‐EM structure of the chain‐elongating E3 ubiquitin ligase UBR5
Z Hodáková, I Grishkovskaya, HL Brunner… - The EMBO …, 2023 - embopress.org
UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …
[HTML][HTML] UBR5 promotes tumor immune evasion through enhancing IFN-γ-induced PDL1 transcription in triple negative breast cancer
Background: The up-regulation of PD-L1 is recognized as an adaption of cancer cells to
evade immune surveillance and attack. However, the intrinsic mechanisms of the induction …
evade immune surveillance and attack. However, the intrinsic mechanisms of the induction …
Structure of the human UBR5 E3 ubiquitin ligase
The human UBR5 is a single polypeptide chain homology to E6AP C terminus (HECT)-type
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …
E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 …
Functional roles of the E3 ubiquitin ligase UBR5 in cancer
RF Shearer, M Iconomou, CKW Watts… - Molecular Cancer …, 2015 - AACR
Abstract The Ubiquitin-Proteasome System (UPS) is an important regulator of cell signaling
and proteostasis, which are essential to a variety of cellular processes. The UPS is disrupted …
and proteostasis, which are essential to a variety of cellular processes. The UPS is disrupted …
[HTML][HTML] Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs
Viruses mimic host short linear motifs (SLiMs) to hijack and deregulate cellular functions.
Studies of motif-mediated interactions therefore provide insight into virus-host …
Studies of motif-mediated interactions therefore provide insight into virus-host …
[HTML][HTML] A conformational switch regulates the ubiquitin ligase HUWE1
B Sander, W Xu, M Eilers, N Popov, S Lorenz - Elife, 2017 - elifesciences.org
The human ubiquitin ligase HUWE1 has key roles in tumorigenesis, yet it is unkown how its
activity is regulated. We present the crystal structure of a C-terminal part of HUWE1 …
activity is regulated. We present the crystal structure of a C-terminal part of HUWE1 …