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

doi:10.1093/pcp/pcw134

	The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases
	Liu, Qing 1,2,3; Wang, Qin 2,3; Liu, Bin 4; Wang, Wei 2; Wang, Xu 2,3; Park, Joon 3; Yang, Zhenming 1; Du, Xinglin 1; Bian, Mingdi 1; Lin, Chentao 1,3
刊名	PLANT AND CELL PHYSIOLOGY
	2016
卷号	57 期号:10 页码:2175-2186
关键词	Arabidopsis thaliana CRY2 Degradation Ubiquitin E3 ligase. edited-statecorrected-proof
ISSN号	0032-0781
DOI	10.1093/pcp/pcw134
通讯作者	Liu, Qing
英文摘要	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 cop15 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 nonpermissive 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.
学科主题	Cell Biology
语种	英语
出版者	OXFORD UNIV PRESS
WOS记录号	WOS:000388374100013
内容类型	期刊论文
源URL	[http://111.203.20.206/handle/2HMLN22E/105309]
专题	作物科学研究所_分子生物学系
作者单位	1.Jilin Univ, Coll Plant Sci, Lab Soil & Plant Mol Genet, Changchun 130062, Peoples R China 2.Fujian Agr & Forestry Univ, Haixia Inst Sci & Technol, Basic Forestry & Prote Res Ctr, Fuzhou 350002, Peoples R China 3.Univ Calif Los Angeles, Dept Mol Cell & Dev Biol, Los Angeles, CA 90095 USA 4.Chinese Acad Agr Sci, Inst Crop Sci, Beijing 100081, Peoples R China
推荐引用方式 GB/T 7714	Liu, Qing,Wang, Qin,Liu, Bin,et al. The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases[J]. PLANT AND CELL PHYSIOLOGY,2016,57(10):2175-2186.
APA	Liu, Qing.,Wang, Qin.,Liu, Bin.,Wang, Wei.,Wang, Xu.,...&Lin, Chentao.(2016).The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases.PLANT AND CELL PHYSIOLOGY,57(10),2175-2186.
MLA	Liu, Qing,et al."The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases".PLANT AND CELL PHYSIOLOGY 57.10(2016):2175-2186.