SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature

被引:10
|
作者
Naranjo-Arcos, Maria [1 ]
Srivastava, Moumita [2 ]
Deligne, Florian [1 ]
Bhagat, Prakash Kumar [2 ]
Mansi, Mansi [2 ]
Sadanandom, Ari [2 ]
Vert, Gregory [1 ]
机构
[1] Univ Toulouse 3, Ctr Natl Rech Sci, Unite Mixte Rech 5546, Plant Sci Res Lab, F-31320 Toulouse, France
[2] Univ Durham, Dept Biosci, Durham DH13LE, Durham, England
关键词
Arabidopsis; SUMO; temperature; BRI1; brassinosteroids; NF-KAPPA-B; EXTRACELLULAR DOMAIN; SIGNAL-TRANSDUCTION; CYTOPLASMIC KINASE; STRUCTURAL BASIS; MODIFIER SUMO; ARABIDOPSIS; AUXIN; ENDOCYTOSIS; ACTIVATION;
D O I
10.1073/pnas.2217255120
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Brassinosteroids (BRs) are a class of steroid molecules perceived at the cell surface that act as plant hormones. The BR receptor BRASSINOSTEROID INSENSITIVE1 (BRI1) offers a model to understand receptor-mediated signaling in plants and the role of post-translational modifications. Here we identify SUMOylation as a new modifi-cation targeting BRI1 to regulate its activity. BRI1 is SUMOylated in planta on two lysine residues, and the levels of BRI1 SUMO conjugates are controlled by the Desi3a SUMO protease. Loss of Desi3a leads to hypersensitivity to BRs, indicating that Desi3a acts as a negative regulator of BR signaling. Besides, we demonstrate that BRI1 is deS-UMOylated at elevated temperature by Desi3a, leading to increased BRI1 interaction with the negative regulator of BR signaling BIK1 and to enhanced BRI1 endocytosis. Loss of Desi3a or BIK1 results in increased response to temperature elevation, indicating that BRI1 deSUMOylation acts as a safety mechanism necessary to keep temperature responses in check. Altogether, our work establishes BRI1 deSUMOylation as a molec-ular crosstalk mechanism between temperature and BR signaling, allowing plants to translate environmental inputs into growth response.
引用
收藏
页数:10
相关论文
共 50 条
  • [21] Autoregulation and homodimerization are involved in the activation of the plant steroid receptor BRI1
    Wang, XL
    Li, XQ
    Meisenhelder, J
    Hunter, T
    Yoshida, S
    Asami, T
    Chory, J
    DEVELOPMENTAL CELL, 2005, 8 (06) : 855 - 865
  • [22] Plant growth: A matter of WAK seeing the wall and talking to BRI1
    Yang, Zhenbiao
    CURRENT BIOLOGY, 2022, 32 (12) : R564 - R566
  • [23] Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1
    Kinoshita, T
    Caño-Delgado, AC
    Seto, H
    Hiranuma, S
    Fujioka, S
    Yoshida, S
    Chory, J
    NATURE, 2005, 433 (7022) : 167 - 171
  • [24] BAK1 Directly Regulates Brassinosteroid Perception and BRI1 Activation
    He, Kai
    Xu, Shengbao
    Li, Jia
    JOURNAL OF INTEGRATIVE PLANT BIOLOGY, 2013, 55 (12) : 1264 - 1270
  • [25] BAK1 Directly Regulates Brassinosteroid Perception and BRI1 Activation
    Kai He
    Shengbao Xu
    Jia Li
    Journal of Integrative Plant Biology, 2013, 55 (12) : 1264 - 1270
  • [26] Brassinosteroid perception and signaling: Heterodimerization and phosphorylation of receptor-like kinases BRI1 and BAK1
    Eckardt, NA
    PLANT CELL, 2005, 17 (06): : 1638 - 1640
  • [27] The brassinosteroid receptor kinase, BRI1, plays a role in seed germination and the release of dormancy by cold stratification
    Kim, Sang Yeol
    Warpeha, Katherine M.
    Huber, Steven C.
    JOURNAL OF PLANT PHYSIOLOGY, 2019, 241
  • [28] The brassinosteroid receptor BRI1 can generate cGMP enabling cGMP-dependent downstream signaling
    Wheeler, Janet I.
    Wong, Aloysius
    Marondedze, Claudius
    Groen, Arnoud J.
    Kwezi, Lusisizwe
    Freihat, Lubna
    Vyas, Jignesh
    Raji, Misjudeen A.
    Irving, Helen R.
    Gehring, Chris
    PLANT JOURNAL, 2017, 91 (04): : 590 - 600
  • [29] The activation of the Arabidopsis P-ATPase 1 by the brassinosteroid receptor BRI1 is independent of threonine 948 phosphorylation
    Witthoeft, Janika
    Caesar, Katharina
    Elgass, Kirstin
    Huppenberger, Peter
    Kilian, Joachim
    Schleifenbaum, Frank
    Oecking, Claudia
    Harter, Klaus
    PLANT SIGNALING & BEHAVIOR, 2011, 6 (07) : 1063 - 1066
  • [30] Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1
    Luo, Yongming
    Takagi, Junpei
    Claus, Lucas Alves Neubus
    Zhang, Chao
    Yasuda, Shigetaka
    Hasegawa, Yoko
    Yamaguchi, Junji
    Shan, Libo
    Russinova, Eugenia
    Sato, Takeo
    EMBO REPORTS, 2022, 23 (04)