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      OST1 kinase modulates freezing tolerance by enhancing ICE1 stability in Arabidopsis.

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          Abstract

          Cold stress is a major environmental factor that limits plant growth and development. The C-repeat-binding factor (CBF)-dependent cold signaling pathway is extensively studied in Arabidopsis; however, the specific protein kinases involved in this pathway remain elusive. Here we report that OST1 (open stomata 1), a well-known Ser/Thr protein kinase in ABA signaling, acts upstream of CBFs to positively regulate freezing tolerance. The ost1 mutants show freezing hypersensitivity, whereas transgenic plants overexpressing OST1 exhibit enhanced freezing tolerance. The OST1 kinase is activated by cold stress. Moreover, OST1 interacts with both the transcription factor ICE1 and the E3 ligase HOS1 in the CBF pathway. Cold-activated OST1 phosphorylates ICE1 and enhances its stability and transcriptional activity. Meanwhile, OST1 interferes with the interaction between HOS1 and ICE1, thus suppressing HOS1-mediated ICE1 degradation under cold stress. Our results thus uncover the unexpected roles of OST1 in modulating CBF-dependent cold signaling in Arabidopsis.

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          Author and article information

          Journal
          Dev. Cell
          Developmental cell
          1878-1551
          1534-5807
          Feb 9 2015
          : 32
          : 3
          Affiliations
          [1 ] State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China.
          [2 ] State Key Laboratory of Plant Genomics and National Plant Gene Research Center, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
          [3 ] State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China. Electronic address: yangshuhua@cau.edu.cn.
          Article
          S1534-5807(14)00844-2
          10.1016/j.devcel.2014.12.023
          25669882
          110c873a-8ae0-4278-bb01-206d89c79b9b
          Copyright © 2015 Elsevier Inc. All rights reserved.
          History

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