期刊
PLANT CELL
卷 26, 期 2, 页码 712-728出版社
OXFORD UNIV PRESS INC
DOI: 10.1105/tpc.113.122234
关键词
-
资金
- Spanish Ministry of Economy and Competitiveness (MINECO)
- National Research Program [BIO2010-18820, BIO2011-29085, BIO2011-23446]
- INNPACTO Program [IPT-310000-2010-9]
- CONSOLIDER Program [2007-28317]
- National Science Foundation [GM-47850]
- National Institutes of Health [GM-47850]
- Formacion de Personal Investigador fellowships from MINECO
- Grants-in-Aid for Scientific Research [25440057] Funding Source: KAKEN
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据