Aug 23, 2024 · The human UBR5 is a single polypeptide chain HECT-type E3 ubiquitin ligase essential for embryonic development in mammals. Dysregulated UBR5 functions like an oncoprotein to promote cancer growth and metastasis. Here we report that UBR5 assembles ...

Human UBR5 is an E3 ubiquitin ligase. Wang et al. discovered that UBR5 exists as dimers and tetramers in solution. They determined the dimer and tetramer structures to high resolution. The structures lay the foundation for elucidating the mechanism of UBR5 activity and developing anticancer drugs targeting the enzyme.

Jul 6, 2023 · One of the largest HECT E3s is UBR5 (also known as EDD or N‐recognin), a nuclear protein containing 2,799 residues in humans. UBR5 was identified as a tumour suppressor gene in Drosophila (Mansfield et al, 1994) and is embryonic lethal upon knockout (Saunders et …

Jul 20, 2023 · Here, we demonstrate the ubiquitin ligase UBR5 drives degradation of multiple agonist-bound NRs, including the retinoic acid receptor alpha (RARA), retinoid x receptor alpha (RXRA), glucocorticoid, estrogen, liver-X, progesterone, and vitamin D receptors.

May 4, 2023 · 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 functions like an oncoprotein to promote cancer growth and metastasis.

Nov 1, 2022 · The human UBR5 (also known as EDD) is a single polypeptide chain HECT-type E3 ubiquitin ligase essential for embryonic development in mammals. Although widely expressed, UBR5 is markedly...

Aug 24, 2023 · We used chemistry and cryo‐electron microscopy (cryo‐EM) to visualize stable mimics of the intermediates along K48-linked Ub chain formation by the human E3, UBR5.

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 functions like an oncoprotein to promote cancer growth and metastasis. Here, we report that UBR5 assembles into a dimer and a tetramer.

Nov 1, 2022 · 94 structure of the human full-length UBR5 at up to 2.66 Å resolution and revealed that UBR5 95 assembles stable dimers and tetramers in solution. The high-resolution structures shed light on the UBR5 catalyzed96 transthiolation reaction mechanism and provide a platform for developing 97 UBR5 inhibitors for the potential treatment of cancers ...

Key points: We have recently identified that a HECT domain E3 ubiquitin ligase, named UBR5, is altered epigenetically (via DNA methylation) after human skeletal muscle hypertrophy, where its gene expression is positively correlated with increasing lean leg mass after training and retraining.