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Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change
Abstract
The E3 ubiquitin (Ub) ligase Itch is a critical regulator of T helper 2 (Th2) cytokine production through its ability to induce Ub-dependent JunB degradation. After T cell receptor engagement, Itch undergoes JNK1-mediated phosphorylation that greatly enhances its enzymatic activity. To investigate how phosphorylation activates an E3 Ub ligase we have identified the JNK1 phosphorylation sites within Itch as S199, S232, and T222, which are located within a Pro-rich region. Phosphorylation of these sites is necessary and sufficient for disrupting an inhibitory interaction between the WW domain of Itch and its catalytic HECT (Homologous to E6-AP C Terminus) domain and induces a conformational change that greatly enhances the catalytic activity of Itch, a HECT E3 ligase found to be directly activated upon its phosphorylation.
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ITCH T222 phosphorylation is observed following NaAsO2 treatment.
“Furthermore, phosphorylation of ITCH at T222, a modification known to enhance its catalytic activity14, was observed following incubation with NaAsO2”
From TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress (2024) · cites this paper as [14]
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Bray, S. J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2009 · Cited by 2,620
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Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates
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System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes
Zhang, W., Wu, K.-P., Sartori, M. A., Kamadurai, H. B., Ordureau, A., Jiang, C., Mercredi, P. Y., Murchie, R., Hu, J., Persaud, A., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.005 · Cited by 168
O’Connor, H. F., & Huibregtse, J. M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2529-6 · Cited by 42
TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress
Jeong, E., Willett, R., Rissone, A., La Spina, M., & Puertollano, R. (2024) · Nature Communications · doi:10.1038/s41467-023-44316-6 · Cited by 25
Metadata
- Authors
- Gallagher, E., Gao, M., Liu, Y.-C., & Karin, M.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-01-30
- Volume
- 103
- Issue
- 6
- Pages
- 1717-1722
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 258
- References
- 1
- Language
- en
- Update notices
- correction (2010-03-19)
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