Solar radiation is the ultimate energy source for all eukaryotes on earth, and it also provides information about the time, season, and surrounding environments. How organisms respond to light and how photosensory receptors mediate light responses represent some of the fundamental questions in biology. Cryptochrome is a blue/UV-A light receptor and the only photoreceptor known to function in both plants and animals. The function of cryptochromes is not limited to the control of plant photomorphogenetic development; their functions in the circadian clock and photoperiodism have also been found to affect complex human health problems such as cancer, sleep disorders, and other behavioral disorders. Investigation of how cryptochromes regulate plant development would increase our understanding of a fundamental aspect of life, and the knowledge resulting from such studies is also relevant to the improvement of human health. We have recently discovered that blue light-induced cryptochrome phosphorylation play key roles in the function and regulation of cryptochromes and identified approximate 100 primary target genes of CRY2 action. We have also developed the new genetics screens to identify mutations affecting cryptochrome functions, including sec (suppressors of cry1cry2), ecc (enhancers of cry1cry2), and coc (CRY2-GFP overexpression counteractor). We have cloned 9 SCC genes, and one ECC gene. The objectives of this proposal are (1) to investigate the biochemical mechanism of cryptochrome phosphorylation; (2) to study how CRY2 affects expressions of its putative primary target genes in response to blue light, and (3) to continue identify and clone the SCC, ECC, and COC genes, and to investigate how the SCC genes that we have identified, especially SCC4-D (a putative RING E3) and SCC5-D (a putative kinase), may mediate cryptochrome signal transduction in Arabidopsis.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM056265-09
Application #
6988848
Study Section
Cellular Signaling and Dynamics Study Section (CSD)
Program Officer
Anderson, James J
Project Start
1997-08-01
Project End
2009-07-31
Budget Start
2005-08-01
Budget End
2006-07-31
Support Year
9
Fiscal Year
2005
Total Cost
$417,150
Indirect Cost
Name
University of California Los Angeles
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
092530369
City
Los Angeles
State
CA
Country
United States
Zip Code
90095
Wang, Qin; Zuo, Zecheng; Wang, Xu et al. (2018) Beyond the photocycle-how cryptochromes regulate photoresponses in plants? Curr Opin Plant Biol 45:120-126
Wang, Qin; Barshop, William D; Bian, Mingdi et al. (2017) The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2. Mol Plant 10:357
Liu, Qing; Wang, Qin; Deng, Weixian et al. (2017) Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2. Nat Commun 8:15234
Yang, Zhaohe; Liu, Bobin; Su, Jun et al. (2017) Cryptochromes Orchestrate Transcription Regulation of Diverse Blue Light Responses in Plants. Photochem Photobiol 93:112-127
Wang, Qin; Zuo, Zecheng; Wang, Xu et al. (2016) Photoactivation and inactivation of Arabidopsis cryptochrome 2. Science 354:343-347
Liu, Qing; Wang, Qin; Liu, Bin et al. (2016) The Blue Light-Dependent Polyubiquitination and Degradation of Arabidopsis Cryptochrome2 Requires Multiple E3 Ubiquitin Ligases. Plant Cell Physiol 57:2175-2186
Liu, Bobin; Yang, Zhaohe; Gomez, Adam et al. (2016) Signaling mechanisms of plant cryptochromes in Arabidopsis thaliana. J Plant Res 129:137-48
Gao, Jie; Wang, Xu; Zhang, Meng et al. (2015) Trp triad-dependent rapid photoreduction is not required for the function of Arabidopsis CRY1. Proc Natl Acad Sci U S A 112:9135-40
Wang, Qin; Barshop, William D; Bian, Mingdi et al. (2015) The blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2. Mol Plant 8:631-43
Wang, Xu; Wang, Qin; Nguyen, Paula et al. (2014) Cryptochrome-mediated light responses in plants. Enzymes 35:167-89

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