Abstract:
:Strigolactones (SLs) are a group of newly identified plant hormones that control plant shoot branching. SL signalling requires the hormone-dependent interaction of DWARF 14 (D14), a probable candidate SL receptor, with DWARF 3 (D3), an F-box component of the Skp-Cullin-F-box (SCF) E3 ubiquitin ligase complex. Here we report the characterization of a dominant SL-insensitive rice (Oryza sativa) mutant dwarf 53 (d53) and the cloning of D53, which encodes a substrate of the SCF(D3) ubiquitination complex and functions as a repressor of SL signalling. Treatments with GR24, a synthetic SL analogue, cause D53 degradation via the proteasome in a manner that requires D14 and the SCF(D3) ubiquitin ligase, whereas the dominant form of D53 is resistant to SL-mediated degradation. Moreover, D53 can interact with transcriptional co-repressors known as TOPLESS-RELATED PROTEINS. Our results suggest a model of SL signalling that involves SL-dependent degradation of the D53 repressor mediated by the D14-D3 complex.
journal_name
Naturejournal_title
Natureauthors
Jiang L,Liu X,Xiong G,Liu H,Chen F,Wang L,Meng X,Liu G,Yu H,Yuan Y,Yi W,Zhao L,Ma H,He Y,Wu Z,Melcher K,Qian Q,Xu HE,Wang Y,Li Jdoi
10.1038/nature12870subject
Has Abstractpub_date
2013-12-19 00:00:00pages
401-5issue
7480eissn
0028-0836issn
1476-4687pii
nature12870journal_volume
504pub_type
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