[HTML][HTML] Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects

M Scheffner, S Kumar - Biochimica et Biophysica Acta (BBA)-Molecular …, 2014 - Elsevier
Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-
terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate …

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 …

UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability

JM Tsai, JD Aguirre, YD Li, J Brown, V Focht, L Kater… - Molecular cell, 2023 - cell.com
Nuclear hormone receptors (NRs) are ligand-binding transcription factors that are widely
targeted therapeutically. Agonist binding triggers NR activation and subsequent degradation …

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 …

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 …

Structure of the human UBR5 E3 ubiquitin ligase

F Wang, Q He, W Zhan, Z Yu, E Finkin-Groner, X Ma… - Structure, 2023 - cell.com
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 …

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 …

Identification of the HECT E3 ligase UBR5 as a regulator of MYC degradation using a CRISPR/Cas9 screen

L Schukur, T Zimmermann, O Niewoehner, G Kerr… - Scientific Reports, 2020 - nature.com
MYC oncoprotein is a multifunctional transcription factor that regulates the expression of a
large number of genes involved in cellular growth, proliferation and metabolism. Altered …

Exploring the “Other” subfamily of HECT E3-ligases for therapeutic intervention

S Singh, J Ng, J Sivaraman - Pharmacology & Therapeutics, 2021 - Elsevier
The HECT E3 ligase family regulates key cellular signaling pathways, with its 28 members
divided into three subfamilies: NEDD4 subfamily (9 members), HERC subfamily (6 …

E3 ubiquitin ligase UBR5 modulates circadian rhythm by facilitating the ubiquitination and degradation of the key clock transcription factor BMAL1

C Duan, Y Li, H Zhi, Y Tian, Z Huang, S Chen… - Acta Pharmacologica …, 2024 - nature.com
The circadian clock is the inner rhythm of life activities and is controlled by a self-sustained
and endogenous molecular clock, which maintains a~ 24 h internal oscillation. As the core …