Journal article
Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3 ligases
Molecular plant
10/24/2014
Handle:
https://hdl.handle.net/2376/104073
PMID: 25343985
Abstract
Controlled stability of proteins is a highly efficient mechanism to direct diverse processes in living cells. A key regulatory system for protein stability is given by the ubiquitin proteasome pathway, which uses E3 ligases to mark specific proteins for degradation. In this work MYB56 is identified as a novel target of a CULLIN3 (CUL3)-based E3 ligase. Its stability depends on the presence of MATH-BTB/POZ (BPM) proteins, which function as substrate adaptors to the E3 ligase. Genetic studies pointed out that MYB56 is a negative regulator of flowering, while BPMs positively affect this developmental program. The interaction between BPMs and MYB56 occurs at the promoter of FLOWERING LOCUS T (FT), a key regulator in initiating flowering in Arabidopsis, and results in instability of MYB56. Overall the work establishes MYB transcription factors as substrates of BPM proteins, and provides novel information on components that participate in controlling the flowering time point in plants.
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Details
- Title
- Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3 ligases
- Creators
- Liyuan Chen - Washington State University, Pullman, WA, 99163, USA current address: Plant Gene Expression Center, UC Berkeley, Albany, CA 94710, USAAnne Bernhardt - Washington State University, Pullman, WA, 99163, USA current address: Robert Koch Institut, 13353 Berlin, GermanyJooHyun Lee - Washington State University, Pullman, WA, 99163, USAHanjo Hellmann - Washington State University, Pullman, WA, 99163, USA hellmann@wsu.edu
- Publication Details
- Molecular plant
- Academic Unit
- Biological Sciences, School of
- Publisher
- England
- Identifiers
- 99900546980901842
- Language
- English
- Resource Type
- Journal article