ArticleThe Journal of biological chemistry2018
Substrate clustering potently regulates the activity of WW-HECT domain-containing ubiquitin ligases.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- SMURF1/2 Are Novel Regulators of WNK1 Stability.Kinases and phosphatases · 2024Article
- Extracellular vesicle surface display of αPD-L1 and αCD3 antibodies via engineered late domain-based scaffold to activate T-cell anti-tumor immunity.Journal of extracellular vesicles · 2024Article
- Review
- Divergent regulation of α-arrestin ARRDC3 function by ubiquitination.Molecular biology of the cell · 2023Article
- Differences in CD80 and CD86 transendocytosis reveal CD86 as a key target for CTLA-4 immune regulation.Nature immunology · 2022Article
- TcpC inhibits neutrophil extracellular trap formation by enhancing ubiquitination mediated degradation of peptidylarginine deiminase 4.Nature communications · 2021Article
- Target-induced clustering activates Trim-Away of pathogens and proteins.Nature structural & molecular biology · 2021Article
- TcpC inhibits toll-like receptor signaling pathway by serving as an E3 ubiquitin ligase that promotes degradation of myeloid differentiation factor 88.PLoS pathogens · 2021Article
- Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021Review
- Predicting PY motif-mediated protein-protein interactions in the Nedd4 family of ubiquitin ligases.PloS one · 2021Article
- Life and Death of Fungal Transporters under the Challenge of Polarity.International journal of molecular sciences · 2020Review
- Tales of tails in transporters.Open biology · 2019Review
- WW domain-mediated regulation and activation of E3 ubiquitin ligase Suppressor of Deltex.The Journal of biological chemistry · 2018Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Nedd4 family of HECT domain-containing E3 ligases ubiquitinate many transcription factors and signaling proteins, and their activity is tightly regulated. Normally, intramolecular interactions curb the catalytic activity of the HECT domain, but these can be broken by the binding of PY motifs, found on substrate molecules and adaptors, to the WW domains characteristic of this E3 ligase family. This raises the prospect of substrates automatically activating the ligases, frustrating the purpose of ligase regulation. Here we show that soluble protein substrates and adaptors such as α arrestins, even with multiple PY elements, cannot activate ligase activity efficiently. However, we found that polymerization or membrane tethering of these substrates dramatically increases the ligase activity both
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