The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
USP15 is a deubiquitylating enzyme for receptor-activated SMADs
Open accessAbstract
The TGFβ pathway is critical for embryonic development and adult tissue homeostasis. On ligand stimulation, TGFβ and BMP receptors phosphorylate receptor-activated SMADs (R-SMADs), which then associate with SMAD4 to form a transcriptional complex that regulates gene expression through specific DNA recognition. Several ubiquitin ligases serve as inhibitors of R-SMADs, yet no deubiquitylating enzyme (DUB) for these molecules has so far been identified. This has left unexplored the possibility that ubiquitylation of R-SMADs is reversible and engaged in regulating SMAD function, in addition to degradation. Here we identify USP15 as a DUB for R-SMADs. USP15 is required for TGFβ and BMP responses in mammalian cells and Xenopus embryos. At the biochemical level, USP15 primarily opposes R-SMAD monoubiquitylation, which targets the DNA-binding domains of R-SMADs and prevents promoter recognition. As such, USP15 is critical for the occupancy of endogenous target promoters by the SMAD complex. These data identify an additional layer of control by which the ubiquitin system regulates TGFβ biology.
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Cites
Nuclear CDKs Drive Smad Transcriptional Activation and Turnover in BMP and TGF-β Pathways
Alarcón, C., Zaromytidou, A.-I., Xi, Q., Gao, S., Yu, J., Fujisawa, S., Barlas, A., Miller, A. N., Manova-Todorova, K., Macias, M. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.035 · Cited by 719
FAM/USP9x, a Deubiquitinating Enzyme Essential for TGFβ Signaling, Controls Smad4 Monoubiquitination
Dupont, S., Mamidi, A., Cordenonsi, M., Montagner, M., Zacchigna, L., Adorno, M., Martello, G., Stinchfield, M. J., Soligo, S., Morsut, L., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.051 · Cited by 494
Self-citationThe establishment of spemann's organizer and patterning of the vertebrate embryo
De Robertis, E. M., Larraín, J., Oelgeschläger, M., & Wessely, O. (2000) · Nature Reviews Genetics · doi:10.1038/35042039 · Cited by 429
Cited by
Deubiquitylating enzymes and drug discovery: emerging opportunities
Harrigan, J. A., Jacq, X., Martin, N. M., & Jackson, S. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.152 · Cited by 940
Specificity, versatility, and control of TGF-β family signaling
Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785
Signaling Receptors for TGF-β Family Members
Heldin, C.-H., & Moustakas, A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022053 · Cited by 711
The TGFbeta Superfamily Signaling Pathway
Weiss, A., & Attisano, L. (2013) · WIREs Developmental Biology · doi:10.1002/wdev.86 · Cited by 561
Aerobic glycolysis tunes YAP/TAZ transcriptional activity
Enzo, E., Santinon, G., Pocaterra, A., Aragona, M., Bresolin, S., Forcato, M., Grifoni, D., Pession, A., Zanconato, F., Guzzo, G., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490379 · Cited by 414
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Metadata
- Authors
- Inui, M., Manfrin, A., Mamidi, A., Martello, G., Morsut, L., Soligo, S., Enzo, E., Moro, S., Polo, S., Dupont, S., Cordenonsi, M., & Piccolo, S.
- Venue
- Nature Cell Biology
- Published
- 2011-09-25
- Volume
- 13
- Issue
- 11
- Pages
- 1368-1375
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2048966465
- Cited by
- 190
- References
- 3
- FWCI
- 6.23
- Type
- journal article
- Language
- en
- Open access
- green
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- Inui, M., Manfrin, A., Mamidi, A., Martello, G., Morsut, L., Soligo, S., Enzo, E., Moro, S., Polo, S., Dupont, S., Cordenonsi, M., & Piccolo, S. (2011). USP15 is a deubiquitylating enzyme for receptor-activated SMADs. Nature Cell Biology. https://doi.org/10.1038/ncb2346
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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