The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1
Open accessAbstract
Steroid receptor co-activator-3 (SRC-3/AIB1) is an oncogene that is amplified and overexpressed in many human cancers. However, the molecular mechanisms that regulate ‘activated SRC-3 oncoprotein’ turnover during tumorigenesis remain to be elucidated. Here, we report that speckle-type POZ protein (SPOP), a cullin 3 (CUL3)-based ubiquitin ligase, is responsible for SRC-3 ubiquitination and proteolysis. SPOP interacts directly with an SRC-3 phospho-degron in a phosphorylation-dependent manner. Casein kinase Iɛ phosphorylates the S102 in this degron and promotes SPOP-dependent turnover of SRC-3. Short hairpin RNA knockdown and overexpression experiments substantiated that the SPOP/CUL3/Rbx1 ubiquitin ligase complex promotes SRC-3 turnover. A systematic analysis of the SPOP genomic locus revealed that a high percentage of genomic loss or loss of heterozygosity occurs at this locus in breast cancers. Furthermore, we demonstrate that restoration of SPOP expression inhibited SRC-3-mediated oncogenic signaling and tumorigenesis, thus positioning SPOP as a tumor suppressor.
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Cites
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Function and regulation of cullin–RING ubiquitin ligases
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Control of Mammalian Circadian Rhythm by CKIε-Regulated Proteasome-Mediated PER2 Degradation
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KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ
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Cited by
The role of ubiquitination in tumorigenesis and targeted drug discovery
Deng, L., Meng, T., Chen, L., Wei, W., & Wang, P. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0107-0 · Cited by 744
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Genschik, P., Sumara, I., & Lechner, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.173 · Cited by 278
Cullin 3 mediates SRC-3 ubiquitination and degradation to control the retinoic acid response
Ferry, C., Gaouar, S., Fischer, B., Boeglin, M., Paul, N., Samarut, E., Piskunov, A., Pankotai-Bodo, G., Brino, L., & Rochette-Egly, C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102572108 · Cited by 33
Thomasen, F. E., Cuneo, M. J., Mittag, T., & Lindorff-Larsen, K. (2023) · eLife · doi:10.7554/elife.84147 · Cited by 9
Metadata
- Authors
- Li, C., Ao, J., Fu, J., Lee, D.-F., Xu, J., Lonard, D., & O'Malley, B. W.
- Venue
- Oncogene
- Published
- 2011-05-16
- Volume
- 30
- Issue
- 42
- Pages
- 4350-4364
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2088643139
- Cited by
- 173
- References
- 7
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- green
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