The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase
Open accessAbstract
Protein kinases have central functions in various cellular signal transduction pathways through their substrate phosphorylation. Here we show that a protein kinase, DYRK2, has unexpected role as a scaffold for an E3 ubiquitin ligase complex. DYRK2 associates with an E3 ligase complex containing EDD, DDB1 and VPRBP proteins (EDVP complex). Strikingly, DYRK2 serves as a scaffold for the EDVP complex, because small-interfering-RNA-mediated depletion of DYRK2 disrupts the formation of the EDD–DDB1–VPRBP complex. Although the kinase activity of DYRK2 is dispensable for its ability to mediate EDVP complex formation, it is required for the phosphorylation and subsequent degradation of its downstream substrate, katanin p60. Collectively, our results reveal a new type of E3-ubiquitin ligase complex in humans that depends on a protein kinase for complex formation as well as for the subsequent phosphorylation, ubiquitylation and degradation of their substrates.
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Cites
Molecular architecture and assembly of the DDB1–CUL4A ubiquitin ligase machinery
Angers, S., Li, T., Yi, X., MacCoss, M. J., Moon, R. T., & Zheng, N. (2006) · Nature · doi:10.1038/nature05175 · Cited by 674
Jin, J., Arias, E. E., Chen, J., Harper, J. W., & Walter, J. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.010 · Cited by 632
Self-citationDCAFs, the Missing Link of the CUL4-DDB1 Ubiquitin Ligase
Lee, J., & Zhou, P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.001 · Cited by 460
Cited by
Merlin/NF2 Suppresses Tumorigenesis by Inhibiting the E3 Ubiquitin Ligase CRL4DCAF1 in the Nucleus
Li, W., You, L., Cooper, J., Schiavon, G., Pepe-Caprio, A., Zhou, L., Ishii, R., Giovannini, M., Hanemann, C. O., Long, S. B., et al. (2010) · Cell · doi:10.1016/j.cell.2010.01.029 · Cited by 321
WWP2 is an E3 ubiquitin ligase for PTEN
Maddika, S., Kavela, S., Rani, N., Palicharla, V. R., Pokorny, J. L., Sarkaria, J. N., & Chen, J. (2011) · Nature Cell Biology · doi:10.1038/ncb2240 · Cited by 305
Self-citationHECT E3 ubiquitin ligases – emerging insights into their biological roles and disease relevance
Wang, Y., Argiles-Castillo, D., Kane, E. I., Zhou, A., & Spratt, D. E. (2020) · Journal of Cell Science · doi:10.1242/jcs.228072 · Cited by 128
Zhang, L., Lian, R., Zhao, J., Feng, X., Ye, R., Pan, L., Wu, J., Li, M., Huang, Y., & Cai, J. (2019) · Cell & Bioscience · doi:10.1186/s13578-019-0310-2 · Cited by 36
Metadata
- Authors
- Maddika, S., & Chen, J.
- Venue
- Nature Cell Biology
- Published
- 2009-03-15
- Volume
- 11
- Issue
- 4
- Pages
- 409-419
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W1981969443
- Cited by
- 177
- References
- 3
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- green
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