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The HECT ubiquitin-protein ligases UPL1 and UPL2 are involved in degradation of Arabidopsis thaliana ACC synthase 7.
Physiol Plant
January 2025
Laboratory of Biotechnology, Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University in Poznań, Poznań, Poland.
Ethylene is an important plant hormone whose production relies on the action of key enzymes, one of which is 1-aminocyclopropane-1-carboxylate synthase (ACS). There are three classes of ACS, which are all partially regulated by degradation through the ubiquitin-proteasome system (UPS), which regulates ethylene production. Arabidopsis has a single class III ACS, ACS7, but although it is known to be degraded by the 26S proteasome, the UPS proteins involved are poorly characterised.
View Article and Find Full Text PDFThe Ubiquitin Ligase HERC2 promotes Ang II-induced cardiac hypertrophy via destabilization of MeCP2 to enhance Lin28a expression.
J Cardiovasc Pharmacol
November 2024
Department of Anaesthesiology, the Second Affiliated Hospital of Nanchang University, Nanchang 330006, Jiangxi Province, China.
Article Synopsis
- HERC2, a type of E3 ubiquitin ligase, is found to be highly active in hypertrophic hearts and promotes cardiac hypertrophy by increasing the expression of Lin28a, an RNA-binding protein involved in heart growth.
- Knockdown of HERC2 alleviates hypertrophy caused by angiotensin II (Ang II), while its overexpression worsens the condition.
- The study suggests that HERC2 influences Lin28a levels through the degradation of MeCP2, a protein that normally suppresses Lin28a, highlighting the potential of targeting this HERC2/MeCP2/Lin28a pathway to treat heart failure.
Thioredoxin-interacting protein (TXNIP) is a substrate of the NEDD4-like E3 ubiquitin-protein ligase WWP1 in cellular redox state regulation of acute myeloid leukemia cells.
Mol Oncol
January 2025
Department of Experimental Medicine, TOR, University of Rome Tor Vergata, Italy.
The HECT-type E3 ubiquitin WWP1 (also known as NEDD4-like E3 ubiquitin-protein ligase WWP1) acts as an oncogenic factor in acute myeloid leukemia (AML) cells. WWP1 overexpression in AML confers a proliferative advantage to leukemic blasts (abnormal immature white blood cells) and counteracts apoptotic cell death and differentiation. In an effort to elucidate the molecular basis of WWP1 oncogenic activities, we identified WWP1 as a previously unknown negative regulator of thioredoxin-interacting protein (TXNIP)-mediated reactive oxygen species (ROS) production in AML cells.
View Article and Find Full Text PDFThe R436Q missense mutation in WWP1 disrupts autoinhibition of its E3 ubiquitin ligase activity, leading to self-degradation and loss of function.
In Vitro Cell Dev Biol Anim
August 2024
Department of Molecular Therapy, National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawahigashi-Cho, Kodaira, Tokyo, 187-8502, Japan.
Muscular dystrophy in the NH-413 chicken is caused by a missense mutation in the WWP1 gene. WWP1 is a HECT-type E3 ubiquitin ligase containing four tandem WW domains that interact with proline-rich peptide motifs of target proteins, and a short region connecting the second and third WW domains is crucial for the E3 ligase to maintain an autoinhibitory state. A mutation of the arginine in the WW2-WW3 linker to glutamine is thought to affect WWP1 function, but there is little information on this mutation to date.
View Article and Find Full Text PDFStructural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1.
Nat Struct Mol Biol
February 2024
Research Group 'Ubiquitin Signaling Specificity', Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Ubiquitin ligases (E3s) are pivotal specificity determinants in the ubiquitin system by selecting substrates and decorating them with distinct ubiquitin signals. However, structure determination of the underlying, specific E3-substrate complexes has proven challenging owing to their transient nature. In particular, it is incompletely understood how members of the catalytic cysteine-driven class of HECT-type ligases (HECTs) position substrate proteins for modification.
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