BLADE-ON-PETIOLE proteins act in an E3 ubiquitin ligase complex to regulate PHYTOCHROME INTERACTING FACTOR 4 abundance.

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22 août 2017

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Périmètre
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Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.26759

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/28826468

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/2050-084X

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_64FE7DD6C3CA7

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Serveur Académique Lausannois

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Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

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Arabidopsis/growth & development; Arabidopsis/radiation effects; Arabidopsis Proteins/metabolism; Basic Helix-Loop-Helix Transcription Factors/metabolism; Carrier Proteins/metabolism; Gene Expression Regulation, Plant; Light; Plant Development/radiation effects; Protein Binding; Temperature; Ubiquitin-Protein Ligases/metabolism; Ubiquitination; A. thaliana; BOP; E3 ligase; PHYB; PIF4; light signalling; plant biology; ubiquitination

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B. Zhang et al., « BLADE-ON-PETIOLE proteins act in an E3 ubiquitin ligase complex to regulate PHYTOCHROME INTERACTING FACTOR 4 abundance. », Serveur académique Lausannois, ID : 10.7554/eLife.26759

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Both light and temperature have dramatic effects on plant development. Phytochrome photoreceptors regulate plant responses to the environment in large part by controlling the abundance of PHYTOCHROME INTERACTING FACTOR (PIF) transcription factors. However, the molecular determinants of this essential signaling mechanism still remain largely unknown. Here, we present evidence that the BLADE-ON-PETIOLE ( BOP ) genes, which have previously been shown to control leaf and flower development in Arabidopsis, are involved in controlling the abundance of PIF4. Genetic analysis shows that BOP2 promotes photo-morphogenesis and modulates thermomorphogenesis by suppressing PIF4 activity, through a reduction in PIF4 protein level. In red-light-grown seedlings PIF4 ubiquitination was reduced in the bop2 mutant. Moreover, we found that BOP proteins physically interact with both PIF4 and CULLIN3A and that a CULLIN3-BOP2 complex ubiquitinates PIF4 in vitro. This shows that BOP proteins act as substrate adaptors in a CUL3 BOP1/BOP2 E3 ubiquitin ligase complex, targeting PIF4 proteins for ubiquitination and subsequent degradation.

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