A Study of the Blue-Light-Dependent Phosphorylation, Degradation, and Photobody Formation of Arabidopsis CRY2

doi:10.1093/mp/sss007

	A Study of the Blue-Light-Dependent Phosphorylation, Degradation, and Photobody Formation of Arabidopsis CRY2
	Zuo, Ze-Cheng 1,3; Meng, Ying-Ying 1; Yu, Xu-Hong 3; Zhang, Zeng-Lin 1; Feng, De-Shun 2; Sun, Shih-Fan 3; Liu, Bin 1; Lin, Chen-Tao 3
刊名	MOLECULAR PLANT
	2012
卷号	5 期号:3 页码:726-733
关键词	protein phosphorylation signal transduction fluorescence imaging protein degradation photobody
ISSN号	1674-2052
DOI	10.1093/mp/sss007
通讯作者	Zuo, Ze-Cheng
英文摘要	Arabidopsis cryptochrome 2 (CRY2) is a blue-light receptor mediating blue-light inhibition of hypocotyl elongation and photoperiodic promotion of floral initiation. CRY2 is a constitutive nuclear protein that undergoes blue-light-dependent phosphorylation, ubiquitination, photobody formation, and degradation in the nucleus, but the relationship between these blue-light-dependent events remains unclear. It has been proposed that CRY2 phosphorylation triggers a conformational change responsible for the subsequent ubiquitination and photobody formation, leading to CRY2 function and/or degradation. We tested this hypothesis by a structure-function study, using mutant CRY2-GFP fusion proteins expressed in transgenic Arabidopsis. We show that changes of lysine residues of the NLS (Nuclear Localization Signal) sequence of CRY2 to arginine residues partially impair the nuclear importation of the CRY2(K541R) and CRY2(K554/5R) mutant proteins, resulting in reduced phosphorylation, physiological activities, and degradation in response to blue light. In contrast to the wild-type CRY2 protein that forms photobodies exclusively in the nucleus, the CRY2(K541R) and CRY2(K554/5R) mutant proteins form protein bodies in both the nucleus and cytosol in response to blue light. These results suggest that photoexcited CRY2 molecules can aggregate to form photobody-like structure without the nucleus-dependent protein modifications or the association with the nuclear CRY2-interacting proteins. Taken together, the observation that CRY2 forms photobodies markedly faster than CRY2 phosphorylation in response to blue light, we hypothesize that the photoexcited cryptochromes form oligomers, preceding other biochemical changes of CRY2, to facilitate photobody formation, signal amplification, and propagation, as well as desensitization by degradation.
学科主题	Biochemistry & Molecular Biology ; Plant Sciences ; BIOCHEMISTRY & MOLECULAR BIOLOGY ; PLANT SCIENCES
语种	英语
出版者	OXFORD UNIV PRESS
WOS记录号	WOS:000304890600020
内容类型	期刊论文
源URL	[http://111.203.20.206/handle/2HMLN22E/5163]
专题	作物科学研究所_分子生物学系
作者单位	1.Chinese Acad Agr Sci, Inst Crop Sci, Beijing 100080, Peoples R China 2.Shandong Agr Univ, Coll Agron, Natl Wheat Improvement Ctr, Natl Key Lab Crop Biol,Taian Subctr, Tai An 271018, Shandong, Peoples R China 3.Univ Calif Los Angeles, Dept Mol Cell & Dev Biol, Los Angeles, CA 90095 USA
推荐引用方式 GB/T 7714	Zuo, Ze-Cheng,Meng, Ying-Ying,Yu, Xu-Hong,et al. A Study of the Blue-Light-Dependent Phosphorylation, Degradation, and Photobody Formation of Arabidopsis CRY2[J]. MOLECULAR PLANT,2012,5(3):726-733.
APA	Zuo, Ze-Cheng.,Meng, Ying-Ying.,Yu, Xu-Hong.,Zhang, Zeng-Lin.,Feng, De-Shun.,...&Lin, Chen-Tao.(2012).A Study of the Blue-Light-Dependent Phosphorylation, Degradation, and Photobody Formation of Arabidopsis CRY2.MOLECULAR PLANT,5(3),726-733.
MLA	Zuo, Ze-Cheng,et al."A Study of the Blue-Light-Dependent Phosphorylation, Degradation, and Photobody Formation of Arabidopsis CRY2".MOLECULAR PLANT 5.3(2012):726-733.