The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The E3 ubiquitin ligase Itch controls the protein stability of p63
Abstract
p63, a member of the p53 family of transcription factors, plays an important role in epithelial development, regulating both cell cycle and apoptosis. Even though p63 activity is regulated mainly at the posttranslational level, the control of p63 protein stability is far from being fully understood. Here, we show that the Hect (homologous to the E6-associated protein C terminus)-containing Nedd4-like ubiquitin protein ligase Itch binds, ubiquitylates, and promotes the degradation of p63. The physical interaction occurs at the border between the PY and the SAM (sterile α motif) domains; a single Y504F mutation significantly affects p63 degradation. Itch and p63 are coexpressed in the epidermis and in primary keratinocytes where Itch controls the p63 protein steady-state level. Accordingly, p63 protein levels are significantly increased in Itch knockout keratinocytes. These data suggest that Itch has a fundamental role in the mechanism that controls endogenous p63 protein levels and therefore contributes to regulation of p63 in physiological conditions.
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Cites
Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line.
Boukamp, P., Petrussevska, R. T., Breitkreutz, D., Hornung, J., Markham, A., & Fusenig, N. E. (1988) · The Journal of cell biology · doi:10.1083/jcb.106.3.761 · Cited by 4,170
Chang, L., Kamata, H., Solinas, G., Luo, J.-L., Maeda, S., Venuprasad, K., Liu, Y.-C., & Karin, M. (2006) · Cell · doi:10.1016/j.cell.2006.01.021 · Cited by 706
TAp63α induces apoptosis by activating signaling via death receptors and mitochondria
Gressner, O., Schilling, T., Lorenz, K., Schulze Schleithoff, E., Koch, A., Schulze‐Bergkamen, H., Maria Lena, A., Candi, E., Terrinoni, A., Valeria Catani, M., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600708 · Cited by 255
Self-citation
Cited by
The HECT Family of E3 Ubiquitin Ligases: Multiple Players in Cancer Development
Bernassola, F., Karin, M., Ciechanover, A., & Melino, G. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.06.001 · Cited by 541
Self-citationmiR-203 represses ‘stemness’ by repressing ΔNp63
Lena, A. M., Shalom-Feuerstein, R., di Val Cervo, P. R., Aberdam, D., Knight, R. A., Melino, G., & Candi, E. (2008) · Cell Death & Differentiation · doi:10.1038/cdd.2008.69 · Cited by 389
Self-citationEndo-lysosomal dysregulations and late-onset Alzheimer’s disease: impact of genetic risk factors
Van Acker, Z. P., Bretou, M., & Annaert, W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0323-7 · Cited by 222
Lopez, R. G., Garcia-Silva, S., Moore, S. J., Bereshchenko, O., Martinez-Cruz, A. B., Ermakova, O., Kurz, E., Paramio, J. M., & Nerlov, C. (2009) · Nature Cell Biology · doi:10.1038/ncb1960 · Cited by 106
p63 in Skin Development and Ectodermal Dysplasias
Koster, M. I. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.119 · Cited by 100
Metadata
- Authors
- Rossi, M., Aqeilan, R. I., Neale, M., Candi, E., Salomoni, P., Knight, R. A., Croce, C. M., & Melino, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2006-08-22
- Volume
- 103
- Issue
- 34
- Pages
- 12753-12758
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2149966409
- Cited by
- 223
- References
- 3
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rossi, M., Aqeilan, R. I., Neale, M., Candi, E., Salomoni, P., Knight, R. A., Croce, C. M., & Melino, G. (2006). The E3 ubiquitin ligase Itch controls the protein stability of p63. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0603449103
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