4.8 Article

UBP12 and UBP13 deubiquitinases destabilize the CRY2 blue light receptor to regulate Arabidopsis growth

期刊

CURRENT BIOLOGY
卷 32, 期 15, 页码 3221-+

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CELL PRESS
DOI: 10.1016/j.cub.2022.05.046

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  1. National Institutes of Health (NIH) [R35GM125003, GM12500303S1, GM12500304S1]

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Light is a crucial signal sensed by CRY receptors to regulate growth and circadian clock. This study uncovers the role of UBP12/13 deubiquitinases in negatively regulating CRY2 and modulating hypocotyl growth. UBP12/13 interacts with COP1 to stabilize it, leading to degradation of CRY2 under blue light. The findings provide insight into the regulation of deubiquitinase activity and its role in controlling plant growth.
Light is a crucial exogenous signal sensed by cryptochrome (CRY) blue light receptors to modulate growth and the circadian clock in plants and animals. However, how CRYs interpret light quantity to regulate growth in plants remains poorly understood. Furthermore, CRY2 protein levels and activity are tightly regulated in light to fine-tune hypocotyl growth; however, details of the mechanisms that explain precise control of CRY2 levels are not fully understood. We show that in Arabidopsis, UBP12 and UBP13 deubiquitinases phys-ically interact with CRY2 in light. UBP12/13 negatively regulates CRY2 by promoting its ubiquitination and turnover to modulate hypocotyl growth. Growth and development were explicitly affected in blue light when UBP12/13 were disrupted or overexpressed, indicating their role alongside CRY2. UBP12/13 also inter-acted with and stabilized COP1, which is partially required for CRY2 turnover. Our combined genetic and mo-lecular data support a mechanistic model in which UBP12/13 interact with CRY2 and COP1, leading to the stabilization of COP1. Stabilized COP1 then promotes the ubiquitination and degradation of CRY2 under blue light. Despite decades of studies on deubiquitinases, the knowledge of how their activity is regulated is limited. Our study provides insight into how exogenous signals and ligands, along with their receptors, regulate deubiquitinase activity by protein-protein interaction. Collectively, our results provide a framework of cryptochromes and deubiquitinases to detect and interpret light signals to control plant growth at the most appropriate time.

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