[HTML][HTML] Emerging functions of branched ubiquitin chains

ME French, CF Koehler, T Hunter - Cell discovery, 2021 - nature.com
Ubiquitylation is a critical post-translational modification that controls a wide variety of
processes in eukaryotes. Ubiquitin chains of different topologies are specialized for different …

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 …

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 …

[HTML][HTML] IL-1β turnover by the UBE2L3 ubiquitin conjugating enzyme and HECT E3 ligases limits inflammation

V Mishra, A Crespo-Puig, C McCarthy… - Nature …, 2023 - nature.com
The cytokine interleukin-1β (IL-1β) has pivotal roles in antimicrobial immunity, but also
incites inflammatory disease. Bioactive IL-1β is released following proteolytic maturation of …

Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization

S Singh, S Machida, NK Tulsian, YK Choong… - Advanced …, 2023 - Wiley Online Library
HACE1 is an ankyrin repeat (AKR) containing HECT‐type E3 ubiquitin ligase that interacts
with and ubiquitinates multiple substrates. While HACE1 is a well‐known tumor suppressor …

Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity

S Singh, J Sivaraman - Biochemical Journal, 2020 - portlandpress.com
The HECT family of E3 ubiquitin ligase is divided into three subfamilies: the NEDD4, the
HERC, and the 'other'. Previous studies have mostly targeted members of the NEDD4 …

A panel of engineered ubiquitin variants targeting the family of domains found in ubiquitin specific proteases (DUSPs)

JQ Tang, G Veggiani, A Singer, J Teyra, J Chung… - Journal of Molecular …, 2021 - Elsevier
Abstract Domains found in ubiquitin specific proteases (DUSPs) occur in seven members of
the ubiquitin specific protease (USP) family. DUSPs are defined by a distinct structural fold …

A review: targeting UBR5 domains to mediate emerging roles and mechanisms: chance or necessity?

Y Wang, K Niu, Y Shi, F Zhou, X Li, Y Li… - … Journal of Surgery, 2024 - journals.lww.com
Ubiquitinases are known to catalyze ubiquitin chains on target proteins to regulate various
physiological functions like cell proliferation, autophagy, apoptosis, and cell cycle …

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family

EI Kane, SA Beasley, JM Schafer, JE Bohl… - Bioscience …, 2022 - portlandpress.com
There are 28 unique human members of the homologous to E6AP C-terminus (HECT) E3
ubiquitin ligase family. Each member of the HECT E3 ubiquitin ligases contains a conserved …

Tom1p ubiquitin ligase structure, interaction with Spt6p, and function in maintaining normal transcript levels and the stability of chromatin in promoters

J Madrigal, HL Schubert, MA Sdano, L McCullough… - bioRxiv, 2024 - biorxiv.org
Phosphorylation-dependent binding of the S. cerevisiae Spt6p tSH2 domain (Spt6ptSH2) to
the Rbp1p subunit of RNA polymerase II supports efficient transcription. Here, we report that …