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| Reversible SUMOylation of FHY1 Regulates Phytochrome A Signaling in Arabidopsis | |
Qu, Gao-Ping; Li, Hong2; Lin, Xiao-Li; Kong, Xiangxiong; Hu, Zi-Liang; Jin, Yin Hua; Liu, Yu1; Song, Hang-Lin; Kim, Dae Heon4; Lin, Rongcheng5 ; Li, Jigang2; Jin, Jing Bo
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| 2020 | |
| Source Publication | MOLECULAR PLANT
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| ISSN | 1674-2052 |
| Volume | 13Issue:6Pages:879-893 |
| Abstract | In response to far-red light (FR), FAR-RED ELONGATED HYPOCOTYL 1 (FHY1) transports the photoactivated phytochrome A (phyA), the primary FR photoreceptor, into the nucleus, where it initiates FR signaling in plants. Light promotes the 26S proteasome-mediated degradation of FHY1, which desensitizes FR signaling, but the underlying regulatory mechanism remains largely unknown. Here, we show that reversible SUMOylation of FHY1 tightly regulates this process. Lysine K32 (K32) and K103 are major SUMOylation sites of FHY1. We found that FR exposure promotes the SUMOylation of FHY1, which accelerates its degradation. Furthermore, we discovered that ARABIDOPSIS SUMO PROTEASE 1 (ASP1) interacts with FHY1 in the nucleus under FR and facilitates its deSUMOylation. FHY1 was strongly SUMOylated and its protein level was decreased in the asp1-1 loss-of-function mutant compared with that in the wild type under FR. Consistently, asp1-1 seedlings exhibited a decreased sensitivity to FR, suggesting that ASP1 plays an important role in the maintenance of proper FHY1 levels under FR. Genetic analysis further revealed that ASP1 regulates FR signaling through an FHY1- and phyA-dependent pathway. Interestingly, We found that continuous FR inhibits ASP1 accumulation, perhaps contributing to the desensitization of FR signaling. Taken together, these results indicate that FR-induced SUMOylation and ASP1-dependent deSUMOylation of FHY1 represent a key regulatory mechanism that fine-tunes FR signaling. |
| Keyword | Arabidopsis photomorphogenesis FHY1 SUMO ASP1 |
| Subject Area | Biochemistry & Molecular Biology ; Plant Sciences |
| DOI | 10.1016/j.molp.2020.04.002 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | RED ELONGATED HYPOCOTYL1 ; LIGHT-INDUCED PHOSPHORYLATION ; SUMO E3 LIGASE ; NUCLEAR ACCUMULATION ; DEGRADATION ; PROTEINS ; PHOTOMORPHOGENESIS ; DESUMOYLATION ; MODULATION ; INHIBITION |
| WOS Research Area | Biochemistry & Molecular Biology ; Plant Sciences |
| WOS ID | WOS:000537943400012 |
| Publisher | CELL PRESS |
| Subtype | Article |
| Publication Place | CAMBRIDGE |
| EISSN | 1752-9867 |
| Funding Organization | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31670186, 31870238] ; Chinese Academy of SciencesChinese Academy of Sciences [ZDRW-ZS-2019-2-0101, KFJ-STS-ZDTP-076-1] ; Chinese Academy of Sciences (The Innovative Academy of Seed Design) |
| Corresponding Author Email | jinjb@ibcas.ac.cn |
| OA | Bronze |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.ibcas.ac.cn/handle/2S10CLM1/21733 |
| Collection | 中科院植物分子生理学重点实验室 |
| Affiliation | 1.Chinese Acad Sci, Inst Bot, Key Lab Plant Mol Physiol, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.China Agr Univ, Coll Biol Sci, State Key Lab Plant Physiol & Biochem, Beijing 100193, Peoples R China 4.Yanbian Acad Agr Sci, Yanji 133001, Peoples R China 5.Sunchon Natl Univ, Dept Biol, Sunchon 57922, South Korea 6.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China |
| Recommended Citation GB/T 7714 | Qu, Gao-Ping,Li, Hong,Lin, Xiao-Li,et al. Reversible SUMOylation of FHY1 Regulates Phytochrome A Signaling in Arabidopsis[J]. MOLECULAR PLANT,2020,13(6):879-893. |
| APA | Qu, Gao-Ping.,Li, Hong.,Lin, Xiao-Li.,Kong, Xiangxiong.,Hu, Zi-Liang.,...&Jin, Jing Bo.(2020).Reversible SUMOylation of FHY1 Regulates Phytochrome A Signaling in Arabidopsis.MOLECULAR PLANT,13(6),879-893. |
| MLA | Qu, Gao-Ping,et al."Reversible SUMOylation of FHY1 Regulates Phytochrome A Signaling in Arabidopsis".MOLECULAR PLANT 13.6(2020):879-893. |
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| 1-s2.0-S167420522030（2483KB） | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | View Application Full Text | |
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