Plant Nuclear Hormone Receptors: A Role for Small Molecules in Protein-Protein Interactions

被引:79
|
作者
Lumba, Shelley [1 ]
Cutler, Sean [2 ,3 ]
McCourt, Peter [1 ]
机构
[1] Univ Toronto, Dept Cell & Syst Biol, Toronto, ON M5S 3B2, Canada
[2] Univ Calif Riverside, Dept Chem, Riverside, CA 92521 USA
[3] Univ Calif Riverside, Ctr Plant Cell Biol, Dept Bot & Plant Sci, Riverside, CA 92521 USA
基金
美国国家科学基金会;
关键词
auxin; jasmonate; gibberellins; abscisic acid; LIGAND-BINDING DOMAIN; LOSS-OF-FUNCTION; ABSCISIC-ACID; PHOSPHATASE; 2C; GIBBERELLIN RECEPTOR; TRANSCRIPTOME ANALYSIS; SIGNAL-TRANSDUCTION; NEGATIVE REGULATOR; GREEN-REVOLUTION; STRUCTURAL BASIS;
D O I
10.1146/annurev-cellbio-100109-103956
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Plant hormones are a group of chemically diverse small molecules that direct processes ranging from growth and development to biotic and abiotic stress responses. Surprisingly, genome analyses suggest that classic animal nuclear hormone receptor homologs do not exist in plants. It now appears that plants have co-opted several protein families to perceive hormones within the nucleus. In one solution to the problem, the hormones auxin and jasmonate (JA) act as "molecular glue" that promotes protein-protein interactions between receptor F-boxes and downstream corepressor targets. In another solution, gibberellins (GAs) bind and elicit a conformational change in a novel soluble receptor family related to hormone-sensitive lipases. Abscisic acid (ABA), like GA, also acts through an allosteric mechanism involving a START-domain protein. The molecular identification of plant nuclear hormone receptors will allow comparisons with animal nuclear receptors and testing of fundamental questions about hormone function in plant development and evolution.
引用
收藏
页码:445 / 469
页数:25
相关论文
共 50 条
  • [21] Targeting Protein-Protein Interaction by Small Molecules
    Jin, Lingyan
    Wang, Weiru
    Fang, Guowei
    ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY, VOL 54, 2014, 54 : 435 - 456
  • [22] Understanding the Role of Flavonoid Based Small Molecules in Modulating the Oncogenic Protein-Protein Interactions: A Quest for Therapeutic Arsenal
    Karmakar, Abhijit
    Mallick, Tamanna
    Fouzder, Chandrani
    Mukhuty, Alpana
    Mondal, Samiran
    Kundu, Rakesh
    Begum, Naznin Ara
    JOURNAL OF MOLECULAR STRUCTURE, 2022, 1248
  • [23] On the role of electrostatics in protein-protein interactions
    Zhang, Zhe
    Witham, Shawn
    Alexov, Emil
    PHYSICAL BIOLOGY, 2011, 8 (03)
  • [24] Protein-protein interactions in plant antioxidant defense
    Melicher, Pavol
    Dvorak, Petr
    Samaj, Jozef
    Takac, Tomas
    FRONTIERS IN PLANT SCIENCE, 2022, 13
  • [25] Exploring Small Molecules Targeting Protein-Protein Interactions (PPIs): Advancements and Future Prospects
    Patil, Sachin P.
    PHARMACEUTICALS, 2023, 16 (12)
  • [26] A mammalian genetic system to screen for small molecules capable of disrupting protein-protein interactions
    Zhao, HF
    Kiyota, T
    Chowdhury, S
    Purisima, E
    Banville, D
    Konishi, Y
    Shen, SH
    ANALYTICAL CHEMISTRY, 2004, 76 (10) : 2922 - 2927
  • [27] Protein-protein interactions at G-protein-coupled receptors
    Milligan, G
    White, JH
    TRENDS IN PHARMACOLOGICAL SCIENCES, 2001, 22 (10) : 513 - 518
  • [28] Characterization of protein-protein interactions at high concentrations by selective conjugation of small molecules to antibodies
    Swartz, Trevor E.
    Kortkhonjia, Ekaterina
    Huggins, Kelly
    Sharma, Vikas K.
    Patapoff, Tom
    Kabakoff, Bruce
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2011, 241
  • [29] Screening-based approaches to identify small molecules that inhibit protein-protein interactions
    Choi, Sehee
    Choi, Kang-Yell
    EXPERT OPINION ON DRUG DISCOVERY, 2017, 12 (03) : 293 - 303
  • [30] Atomic Interactions and Profile of Small Molecules Disrupting Protein-Protein Interfaces: the TIMBAL Database
    Higueruelo, Alicia P.
    Schreyer, Adrian
    Bickerton, G. Richard J.
    Pitt, Will R.
    Groom, Colin R.
    Blundell, Tom L.
    CHEMICAL BIOLOGY & DRUG DESIGN, 2009, 74 (05) : 457 - 467