4.7 Article

Blue Light-Induced Proteomic Changes in Etiolated Arabidopsis Seedlings

期刊

JOURNAL OF PROTEOME RESEARCH
卷 13, 期 5, 页码 2524-2533

出版社

AMER CHEMICAL SOC
DOI: 10.1021/pr500010z

关键词

Arabidopsis; blue light; phototropins; protein phosphorylation; signal transduction

资金

  1. National Science Foundation [0843617]
  2. Ministry of Science and Technology of China (973 program grant) [2013CB127101]
  3. Zhejiang Natural Science Foundation [LR12C02002]
  4. Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-FG02-08ER15973]
  5. National Institutes of Health [R01GM066258]
  6. Alexander von Humboldt-Foundation, Bonn, Germany (AvH-Fellowships Stanford, University of Kassel, Germany)
  7. Biomedical Research Technology Program of the NIH National Center for Research Resources, NIH NIGMS [8P41GM103481, 1S10RR019934]
  8. Direct For Biological Sciences
  9. Div Of Molecular and Cellular Bioscience [0843617] Funding Source: National Science Foundation
  10. U.S. Department of Energy (DOE) [DE-FG02-08ER15973] Funding Source: U.S. Department of Energy (DOE)

向作者/读者索取更多资源

Plants adapt to environmental light conditions by photoreceptor-mediated physiological responses, but the mechanism by which photoreceptors perceive and transduce the signals is still unresolved. Here, we used 2D difference gel electrophoresis (2D DIGE) and mass spectrometry to characterize early molecular events induced by short blue light exposures in etiolated Arabidopsis seedlings. We observed the phosphorylation of phototropin 1 (phot1) and accumulation of weak chloroplast movement under blue light 1 (WEB1) in the membrane fraction after blue light irradiation. Over 50 spots could be observed for the two rows of phot1 spots in the 2-DE gels, and eight novel phosphorylated Ser/Thr sites were identified in the N-terminus and Hinge 1 regions of phot1 in vivo. Blue light caused ubiquitination of phot1, and K526 of phot1 was identified as a putative ubiquitination site. Our study indicates that post-translational modification of phot1 is more complex than previously reported.

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