Post-translational modifications regulate the activity of the growth-restricting protease DA1

© The Author(s) 2021. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 72(2021), 9 vom: 13. Apr., Seite 3352-3366
1. Verfasser: Chen, Ying (VerfasserIn)
Weitere Verfasser: Inzé, Dirk, Vanhaeren, Hannes
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Review Cell proliferation DA1 N-degron pathway degradation development organ size phosphorylation mehr... protease proteostasis ubiquitination Plant Proteins Peptide Hydrolases EC 3.4.-
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520 |a Plants are a primary food source and can form the basis for renewable energy resources. The final size of their organs is by far the most important trait to consider when seeking increased plant productivity. Being multicellular organisms, plant organ size is mainly determined by the coordination between cell proliferation and cell expansion. The protease DA1 limits the duration of cell proliferation and thereby restricts final organ size. Since its initial identification as a negative regulator of organ growth, various transcriptional regulators of DA1, but also interacting proteins, have been identified. These interactors include cleavage substrates of DA1, and also proteins that modulate the activity of DA1 through post-translational modifications, such as ubiquitination, deubiquitination, and phosphorylation. In addition, many players in the DA1 pathway display conserved phenotypes in other dicot and even monocot species. In this review, we provide a timely overview of the complex, but intriguing, molecular mechanisms that fine-tune the activity of DA1 and therefore final organ size. Moreover, we lay out a roadmap to identify and characterize substrates of proteases and frame the substrate cleavage events in their biological context 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Review 
650 4 |a Cell proliferation 
650 4 |a DA1 
650 4 |a N-degron pathway 
650 4 |a degradation 
650 4 |a development 
650 4 |a organ size 
650 4 |a phosphorylation 
650 4 |a protease 
650 4 |a proteostasis 
650 4 |a ubiquitination 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Peptide Hydrolases  |2 NLM 
650 7 |a EC 3.4.-  |2 NLM 
700 1 |a Inzé, Dirk  |e verfasserin  |4 aut 
700 1 |a Vanhaeren, Hannes  |e verfasserin  |4 aut 
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