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Plant Cell Physiol. 2016 Oct;57(10):2175-2186. Epub 2016 Aug 11.

The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases.

Liu Q1,2,3, Wang Q2,3, Liu B4, Wang W2, Wang X2,3, Park J3, Yang Z1, Du X5, Bian M5, Lin C1,3.

Author information

1
Laboratory of Soil and Plant Molecular Genetics, College of Plant Science, Jilin University, Changchun 130062, China.
2
Basic Forestry and Proteomics Research Center, Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
3
Department of Molecular, Cell & Developmental Biology, University of California, Los Angeles, CA 90095, USA.
4
Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
5
Laboratory of Soil and Plant Molecular Genetics, College of Plant Science, Jilin University, Changchun 130062, China bianmingdiucla@163.com xldu@jlu.edu.cn.

Abstract

Cryptochromes are blue light receptors regulated by light-dependent ubiquitination and degradation in both plant and animal lineages. The Arabidopsis genome encodes two cryptochromes, CRY1 and CRY2, of which CRY2 undergoes blue light-dependent ubiquitination and 26S proteasome-dependent degradation. The molecular mechanism regulating blue light-dependent proteolysis of CRY2 is still not fully understood. We found that the F-box proteins ZEITLUPE (ZTL) and Lov Kelch Protein2 (LKP2), which mediate blue light suppression of degradation of the CRY2 signaling partner CIB1, are not required for the blue light-dependent CRY2 degradation. We further showed that the previously reported function of the COP1-SPA1 protein complex in blue light-dependent CRY2 degradation is more likely to be attributable to its cullin 4 (CUL4)-based E3 ubiquitin ligase activity than its activity as the cryptochrome signaling partner. However, the blue light-dependent CRY2 degradation is only partially impaired in the cul4 mutant, the cop1-5 null mutant and the spa1234 quadruple mutant, suggesting a possible involvement of additional E3 ubiquitin ligases in the regulation of CRY2. Consistent with this hypothesis, we demonstrated that the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature. Based on these and other results presented, we propose that photoexcited CRY2 undergoes Lys48-linked polyubiquitination catalyzed by the CUL4- and CUL1-based E3 ubiquitin ligases.

KEYWORDS:

Arabidopsis thaliana; CRY2; Degradation; Ubiquitin E3 ligase

PMID:
27516416
PMCID:
PMC6083963
DOI:
10.1093/pcp/pcw134
[Indexed for MEDLINE]
Free PMC Article

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