期刊
CELL RESEARCH
卷 25, 期 11, 页码 1219-1236出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/cr.2015.122
关键词
Strigolactones; D14; D3; GR24; receptor/co-receptor
类别
资金
- Van Andel Research Institute, Amway (China)
- National Natural Science Foundation of China [NSFC 31300245, NSFC 91217311]
- Ministry of Science and Technology of China [2012ZX09301001, 2012CB910403, 2013CB910600, XDB08020303, 2013ZX09507001]
- National Institute of Health (USA) [DK071662, GM102545, GM104212]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085P1000817]
- Office of Science of the US Department of Energy [DE-AC02-06CH11357]
Strigolactones (SLs) are endogenous hormones and exuded signaling molecules in plant responses to low levels of mineral nutrients. Key mediators of the SL signaling pathway in rice include the alpha/beta-fold hydrolase DWARF 14 (D14) and the F-box component DWARF 3 (D3) of the ubiquitin ligase SCFD3 that mediate ligand-dependent degradation of downstream signaling repressors. One perplexing feature is that D14 not only functions as the SL receptor but is also an active enzyme that slowly hydrolyzes diverse natural and synthetic SLs including GR24, preventing the crystallization of a binary complex of D14 with an intact SL as well as the ternary D14/SL/D3 complex. Here we overcome these barriers to derive a structural model of D14 bound to intact GR24 and identify the interface that is required for GR24-mediated D14-D3 interaction. The mode of GR24-mediated signaling, including ligand recognition, hydrolysis by D14, and ligand-mediated D14-D3 interaction, is conserved in structurally diverse SLs. More importantly, D14 is destabilized upon the binding of ligands and D3, thus revealing an unusual mechanism of SL recognition and signaling, in which the hormone, the receptor, and the downstream effectors are systematically destabilized during the signal transduction process.
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