The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Identification of SCF Ubiquitin Ligase Substrates by Global Protein Stability Profiling
Abstract
Ubiquitin-mediated proteolysis regulates all aspects of cellular function, and defects in this process are associated with human diseases. The limited number of identified ubiquitin ligase–substrate pairs is a major bottleneck in the ubiquitin field. We established and applied genetic technologies that combine global protein stability (GPS) profiling and genetic perturbation of E3 activity to screen for substrates of the Skp1–cullin–F-box (SCF) ubiquitin ligase in mammalian cells. Among the >350 potential substrates identified, we found most known SCF targets and many previously unknown substrates involved in cell cycle, apoptosis, and signaling pathways. Exploring cell cycle–stage stability, we found that several substrates used the SCF and other E3s in different cell cycle stages. Our results demonstrate the potential of these technologies as general platforms for the global discovery of E3-substrate regulatory networks.
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Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex
Zheng, N., Schulman, B. A., Song, L., Miller, J. J., Jeffrey, P. D., Wang, P., Chu, C., Koepp, D. M., Elledge, S. J., Pagano, M., et al. (2002) · Nature · doi:10.1038/416703a · Cited by 1,507
Self-citationThe SCF ubiquitin ligase: insights into a molecular machine
Cardozo, T., & Pagano, M. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1471 · Cited by 1,114
Kang, J.-S., Tian, J.-H., Pan, P.-Y., Zald, P., Li, C., Deng, C., & Sheng, Z.-H. (2008) · Cell · doi:10.1016/j.cell.2007.11.024 · Cited by 598
Global Protein Stability Profiling in Mammalian Cells
Yen, H.-C. S., Xu, Q., Chou, D. M., Zhao, Z., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1160489 · Cited by 482
Self-citation
Cited by
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A., Sowa, M. E., Rad, R., Rush, J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,613
The Cullin-RING Ubiquitin-Protein Ligases
Hua, Z., & Vierstra, R. D. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112256 · Cited by 511
Global Protein Stability Profiling in Mammalian Cells
Yen, H.-C. S., Xu, Q., Chou, D. M., Zhao, Z., & Elledge, S. J. (2008) · Science · doi:10.1126/science.1160489 · Cited by 482
Self-citationDifferential Diffusivity of Nodal and Lefty Underlies a Reaction-Diffusion Patterning System
Müller, P., Rogers, K. W., Jordan, B. M., Lee, J. S., Robson, D., Ramanathan, S., & Schier, A. F. (2012) · Science · doi:10.1126/science.1221920 · Cited by 381
Metadata
- Authors
- Yen, H.-C. S., & Elledge, S. J.
- Venue
- Science
- Published
- 2008-11-07
- Volume
- 322
- Issue
- 5903
- Pages
- 923-929
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2100547839
- Cited by
- 208
- References
- 5
- FWCI
- 6.58
- Type
- journal article
- Language
- en
- Open access
- closed
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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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