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
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
Function and regulation of cullin–RING ubiquitin ligases
Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084
Control of Mammalian Circadian Rhythm by CKIε-Regulated Proteasome-Mediated PER2 Degradation
Eide, E. J., Woolf, M. F., Kang, H., Woolf, P., Hurst, W., Camacho, F., Vielhaber, E. L., Giovanni, A., & Virshup, D. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.7.2795-2807.2005 · Cited by 495
Zhuang, M., Calabrese, M. F., Liu, J., Waddell, M. B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.022 · Cited by 486
KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ
Lee, D.-F., Kuo, H.-P., Liu, M., Chou, C.-K., Xia, W., Du, Y., Shen, J., Chen, C.-T., Huo, L., Hsu, M.-C., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.025 · Cited by 399 · cited 1×
“…also is vital to many other signaling pathways containing either androgen receptor, progesterone receptor, or transcription factors such as AP-1, E2F1, NF-κB, STAT, TEF-4 and ER81 (Belandia and Parker, 2000; Goel and Janknecht, 2004; Lee et al., 1998; Louie et al., 2004; Werbajh et al., 2000).”
BackgroundSelf-citationGoel, A., & Janknecht, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400036200 · Cited by 95
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
NIH Intramural Sequencing Center (NISC) Comparative Sequencing Program, Le Gallo, M., O'Hara, A. J., Rudd, M. L., Urick, M. E., Hansen, N. F., O'Neil, N. J., Price, J. C., Zhang, S., England, B. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.2455 · Cited by 419
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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- Li, C., Ao, J., Fu, J., Lee, D.-F., Xu, J., Lonard, D., & O'Malley, B. W. (2011). Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1. Oncogene. https://doi.org/10.1038/onc.2011.151
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