This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 20/1/152    most recent tpc.107.055418v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (9) Citing Articles via Google Scholar Google Scholar Articles by Lee, J.-H. Articles by Deng, X. W. Search for Related Content PubMed PubMed Citation Articles by Lee, J.-H. Articles by Deng, X. W. Agricola Articles by Lee, J.-H. Articles by Deng, X. W.

Characterization of Arabidopsis and Rice DWD Proteins and Their Roles as Substrate Receptors for CUL4-RING E3 Ubiquitin Ligases^[W]

^a Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520-8104
^b Department of Biology, Wilkes University, Wilkes-Barre, Pennsylvania 18766
^c Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 27599

² Address correspondence to xingwang.deng{at}yale.edu.

A subset of WD40 proteins that contain a DWD motif (for DDB1 binding WD40) is reported to act as substrate receptors for DDB1-CUL4-ROC1 (for Damaged DNA Binding 1–Cullin 4–Regulator of Cullins 1) based E3 ubiquitin ligases in humans. Here, we report 85 Arabidopsis thaliana and 78 rice (Oryza sativa) proteins containing the conserved 16–amino acid DWD motif. We show by yeast two-hybrid and in vivo coimmunoprecipitation that 11 Arabidopsis DWD proteins directly interact with DDB1 and thus may serve as substrate receptors for the DDB1–CUL4 machinery. We further examine whether the DWD protein PRL1 (for Pleiotropic Regulatory Locus 1) may act as part of a CUL4-based E3 ligase. PRL1 directly interacts with DDB1, and prl1 and cul4cs mutants exhibited similar phenotypes, including altered responses to a variety of stimuli. Moreover, AKIN10 (for Arabidopsis SNF1 Kinase Homolog 10) was degraded more slowly in cell extracts of prl1 and cul4cs than in cell extracts of the wild type. Thus, both genetic and biochemical analyses support the conclusion that PRL1 is the substrate receptor of a CUL4-ROC1-DDB1-PRL1 E3 ligase involved in the degradation of AKIN10. This work adds a large new family to the current portfolio of plant E3 ubiquitin ligases.

This article has been cited by other articles:

				E. Baena-Gonzalez Energy Signaling in the Regulation of Gene Expression during Stress Mol Plant, January 15, 2010; (2010) ssp113v1. [Abstract] [Full Text] [PDF]

				U. Flores-Perez, J. Perez-Gil, M. Closa, L. P. Wright, P. Botella-Pavia, M. A. Phillips, A. Ferrer, J. Gershenzon, and M. Rodriguez-Concepcion PLEIOTROPIC REGULATORY LOCUS 1 (PRL1) Integrates the Regulation of Sugar Responses with Isoprenoid Metabolism in Arabidopsis Mol Plant, January 1, 2010; 3(1): 101 - 112. [Abstract] [Full Text] [PDF]

				T. Chung, D. Wang, C.-S. Kim, R. Yadegari, and B. A. Larkins Plant SMU-1 and SMU-2 Homologues Regulate Pre-mRNA Splicing and Multiple Aspects of Development Plant Physiology, November 1, 2009; 151(3): 1498 - 1512. [Abstract] [Full Text] [PDF]

				K. P. Choe, A. J. Przybysz, and K. Strange The WD40 Repeat Protein WDR-23 Functions with the CUL4/DDB1 Ubiquitin Ligase To Regulate Nuclear Abundance and Activity of SKN-1 in Caenorhabditis elegans Mol. Cell. Biol., May 15, 2009; 29(10): 2704 - 2715. [Abstract] [Full Text] [PDF]

				S. Fragoso, L. Espindola, J. Paez-Valencia, A. Gamboa, Y. Camacho, E. Martinez-Barajas, and P. Coello SnRK1 Isoforms AKIN10 and AKIN11 Are Differentially Regulated in Arabidopsis Plants under Phosphate Starvation Plant Physiology, April 1, 2009; 149(4): 1906 - 1916. [Abstract] [Full Text] [PDF]

				J. Stuttmann, E. Lechner, R. Guerois, J. E. Parker, L. Nussaume, P. Genschik, and L. D. Noel COP9 Signalosome- and 26S Proteasome-dependent Regulation of SCFTIR1 Accumulation in Arabidopsis J. Biol. Chem., March 20, 2009; 284(12): 7920 - 7930. [Abstract] [Full Text] [PDF]

				E. A. Ananieva, G. E. Gillaspy, A. Ely, R. N. Burnette, and F. L. Erickson Interaction of the WD40 Domain of a Myoinositol Polyphosphate 5-Phosphatase with SnRK1 Links Inositol, Sugar, and Stress Signaling Plant Physiology, December 1, 2008; 148(4): 1868 - 1882. [Abstract] [Full Text] [PDF]

				Y. Zhang, S. Feng, F. Chen, H. Chen, J. Wang, C. McCall, Y. Xiong, and X. W. Deng Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 Forms a Nuclear E3 Ubiquitin Ligase with DDB1 and CUL4 That Is Involved in Multiple Plant Developmental Processes PLANT CELL, June 1, 2008; 20(6): 1437 - 1455. [Abstract] [Full Text] [PDF]