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Targeted degradation of abscisic acid receptors is mediated by the ubiquitin ligase substrate adaptor DDA1 in Arabidopsis

By María Luisa Irigoyen, Elisa Iniesto, Leisa Natacha Rodríguez Solovey, Maria Isabel Puga, Yuki Yanagawa, Elah Pick, Elizabeth Strickland, Javier Paz-Ares, Ning Wei, Geert De Jaeger, Pedro Luís Rodríguez Egea, Xing Wang Deng and Vicente Rubio

Abstract

[EN] CULLIN4-RING E3 ubiquitin ligases (CRL4s) regulate key developmental and stress responses in eukaryotes. Studies in both animals and plants have led to the identification of many CRL4 targets as well as specific regulatory mechanisms that modulate their function. The latter involve COP10-DET1-DDB1 (CDD)-related complexes, which have been proposed to facilitate target recognition by CRL4, although the molecular basis for this activity remains largely unknown. Here, we provide evidence that Arabidopsis thaliana DET1-, DDB1-ASSOCIATED1 (DDA1), as part of the CDD complex, provides substrate specificity for CRL4 by interacting with ubiquitination targets. Thus, we show that DDA1 binds to the abscisic acid (ABA) receptor PYL8, as well as PYL4 and PYL9, in vivo and facilitates its proteasomal degradation. Accordingly, we found that DDA1 negatively regulates ABA-mediated developmental responses, including inhibition of seed germination, seedling establishment, and root growth. All other CDD components displayed a similar regulatory function, although they did not directly interact with PYL8. Interestingly, DDA1-mediated destabilization of PYL8 is counteracted by ABA, which protects PYL8 by limiting its polyubiquitination. Altogether, our data establish a function for DDA1 as a substrate receptor for CRL4-CDD complexes and uncover a mechanism for the desensitization of ABA signaling based on the regulation of ABA receptor stability.This research was supported by the Spanish Ministry of Economy and Competitiveness (MINECO; National Research Program, Grants BIO2010-18820 to V. R., BIO2011-29085 to J.P.-A., and BIO2011-23446 to P.L.R.; INNPACTO Program, Grant IPT-310000-2010-9 to J.P.-A.; and CONSOLIDER Program, Grant 2007-28317 to J.P.-A.), the National Science Foundation (Grant GM-47850 to X. W. D.), and the National Institutes of Health (Grant GM-47850 to X. W. D.). E. I. and L. R. were recipients of Formacion de Personal Investigador fellowships from MINECO.Irigoyen, ML.; Iniesto, E.; Rodríguez Solovey, LN.; Puga, MI.; Yanagawa, Y.; Pick, E.; Strickland, E.... (2014). Targeted degradation of abscisic acid receptors is mediated by the ubiquitin ligase substrate adaptor DDA1 in Arabidopsis. Plant Cell. 26(2):712-728. doi:10.​1105/​tpc.​113.​122234S71272826

Topics: Tandem affinity purification, Finger E3 ligase, ABA signal-transduction, Transcription factor, Negative regulator, Positive regulator, Plant transformation, Seed germination, Stress responses, Cop9 signalosome, BIOQUIMICA Y BIOLOGIA MOLECULAR
Publisher: 'American Society of Plant Biologists (ASPB)'
Year: 2014
DOI identifier: 10.1105/tpc.113.122234
OAI identifier: oai:riunet.upv.es:10251/82480
Provided by: RiuNet
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