Physiological functions of the HECT family of ubiquitin ligases
D Rotin, S Kumar - Nature reviews Molecular cell biology, 2009 - nature.com
The ubiquitylation of proteins is carried out by E1, E2 and E3 (ubiquitin ligase) enzymes, and
targets them for degradation or for other cellular fates. The HECT enzymes, including Nedd4 …
targets them for degradation or for other cellular fates. The HECT enzymes, including Nedd4 …
[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 …
terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate …
[HTML][HTML] Tumor derived UBR5 promotes ovarian cancer growth and metastasis through inducing immunosuppressive macrophages
Immunosuppressive tumor microenvironment (TME) and ascites-derived spheroids in
ovarian cancer (OC) facilitate tumor growth and progression, and also pose major obstacles …
ovarian cancer (OC) facilitate tumor growth and progression, and also pose major obstacles …
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] TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes
Histone ubiquitylation is a prominent response to DNA double-strand breaks (DSBs), but
how these modifications are confined to DNA lesions is not understood. Here, we show that …
how these modifications are confined to DNA lesions is not understood. Here, we show that …
[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 …
A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons
A subset of proteins targeted by the N-end rule pathway bear degradation signals called N-
degrons, whose determinants include destabilizing N-terminal residues. Our previous work …
degrons, whose determinants include destabilizing N-terminal residues. Our previous work …
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 …
E3 ubiquitin ligase UBR5 drives the growth and metastasis of triple-negative breast cancer
Patients with triple-negative breast cancers (TNBC) are at high risk for recurrence and
metastasis at an early time despite standard treatment, underscoring the need for novel …
metastasis at an early time despite standard treatment, underscoring the need for novel …
Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase
S Maddika, J Chen - Nature cell biology, 2009 - nature.com
Protein kinases have central functions in various cellular signal transduction pathways
through their substrate phosphorylation. Here we show that a protein kinase, DYRK2, has …
through their substrate phosphorylation. Here we show that a protein kinase, DYRK2, has …