The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction
Open accessAbstract
To elucidate potential roles of CUL4-DDB1-DWD (for Cullin 4-Damaged DNA Binding1-DDB1 binding WD40) E3 ligases in abscisic acid (ABA) signaling, we examined ABA sensitivities of T-DNA mutants of a number of Arabidopsis thaliana DWD genes, which encode substrate receptors for CUL4 E3 ligases. Mutants in two DWD genes, DWA1 and DWA2 (DWD hypersensitive to ABA1 and 2), had ABA-hypersensitive phenotypes. Both proteins interacted with DDB1 in yeast two-hybrid assays and associated with DDB1 and CUL4 in vivo, implying they could form CUL4-based complexes. Several ABA-responsive genes were hyperinduced in both mutants, and the ABA-responsive transcription factors ABA INSENSITIVE 5 (ABI5) and MYC2 accumulated to high levels in the mutants after ABA treatment. Moreover, ABI5 interacted with DWA1 and DWA2 in vivo. Cell-free degradation assays showed ABI5 was degraded more slowly in dwa1 and dwa2 than in wild-type cell extracts. Therefore, DWA1 and/or DWA2 may be the substrate receptors for a CUL4 E3 ligase that targets ABI5 for degradation. Our data indicate that DWA1 and DWA2 can directly interact with each other, and their double mutants exhibited enhanced ABA and NaCl hypersensitivities, implying they can act together. This report thus describes a previously unknown heterodimeric cooperation between two independent substrate receptors for CUL4-based E3 ligases.
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Liu, Q., Kasuga, M., Sakuma, Y., Abe, H., Miura, S., Yamaguchi-Shinozaki, K., & Shinozaki, K. (1998) · The Plant Cell · doi:10.1105/tpc.10.8.1391 · Cited by 3,044
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
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
CDD: a Conserved Domain Database for protein classification
Marchler-Bauer, A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki069 · Cited by 1,156
Chung, K. K. K., Zhang, Y., Lim, K. L., Tanaka, Y., Huang, H., Gao, J., Ross, C. A., Dawson, V. L., & Dawson, T. M. (2001) · Nature Medicine · doi:10.1038/nm1001-1144 · Cited by 750
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
Kamura, T., Sato, S., Haque, D., Liu, L., Kaelin, W. G., Conaway, R. C., & Conaway, J. W. (1998) · Genes & Development · doi:10.1101/gad.12.24.3872 · Cited by 595
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Skubacz, A., Daszkowska-Golec, A., & Szarejko, I. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01884 · Cited by 499
Protein degradation – an alternative respiratory substrate for stressed plants
Araújo, W. L., Tohge, T., Ishizaki, K., Leaver, C. J., & Fernie, A. R. (2011) · Trends in Plant Science · doi:10.1016/j.tplants.2011.05.008 · Cited by 438
E3 Ubiquitin Ligases: Ubiquitous Actors in Plant Development and Abiotic Stress Responses
Shu, K., & Yang, W. (2017) · Plant and Cell Physiology · doi:10.1093/pcp/pcx071 · Cited by 322
Metadata
- Authors
- Lee, J.-H., Yoon, H.-J., Terzaghi, W., Martinez, C., Dai, M., Li, J., Byun, M.-O., & Deng, X. W.
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-06-01
- Volume
- 22
- Issue
- 6
- Pages
- 1716-1732
- ISSN
- 1040-4651 (ISSN-L)
- 1532-298X
- OpenAlex
- W2154368075
- Cited by
- 269
- References
- 8
- FWCI
- 13.10
- Type
- journal article
- Language
- en
- Open access
- bronze
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- The paper
- Lee, J.-H., Yoon, H.-J., Terzaghi, W., Martinez, C., Dai, M., Li, J., Byun, M.-O., & Deng, X. W. (2010). DWA1 and DWA2, Two Arabidopsis DWD Protein Components of CUL4-Based E3 Ligases, Act Together as Negative Regulators in ABA Signal Transduction. The Plant Cell. https://doi.org/10.1105/tpc.109.073783
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