Abstract
Ubiquitylation is a reversible post-translational modification that is involved in various cellular pathways and that thereby regulates various aspects of plant biology. For a long time, functional studies of ubiquitylation have focused on the function of ubiquitylating enzymes, especially the E3 ligases, rather than deubiquitylating enzymes (DUBs) or ubiquitin isopeptidases, enzymes that hydrolyze ubiquitin chains. One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets. However, recent studies have revealed that DUBs also actively participate in controlling cellular events and thus play pivotal roles in plant development and growth. DUBs are also essential for processing ubiquitin precursors and are important for recycling ubiquitin molecules from target proteins prior to their degradation and thereby maintaining the free ubiquitin pool in the cell. Here, we will discuss the five different DUB families (USP/UBP, UCH, JAMM, OTU, and MJD) and their known biochemical and physiological roles in plants.
Highlights
Post-translational modification through ubiquitin, or ubiquitylation, plays a key role in many aspects of plant development, growth and environmental- as well as immune responses
The ubiquitylation status of the substrate proteins is controlled by the activity of deubiquitylating enzymes (DUBs: deubiquitinating enzymes or deubiquitinases), hydrolases that remove covalently attached ubiquitin molecules from substrates or hydrolyze the peptide bond between ubiquitin molecules
Whereas the Arabidopsis genome encodes more than 1500 E3s (Vierstra, 2012), only around 50 DUBs can be identified. This may owe to the fact that in order to deubiquitylate their targets, DUBs may not need direct interaction with the target proteins themselves but rather interact with the ubiquitin chains and DUBs can deal with a broader range of ubiquitylated target proteins
Summary
Edited by: Hongyong Fu, Institute of Plant and Microbial Biology – Academia Sinica, Taiwan. Reviewed by: Wolfgang Schmidt, Academia Sinica, Taiwan Jan Smalle, University of Kentucky, USA. Ubiquitylation is a reversible post-translational modification that is involved in various cellular pathways and that thereby regulates various aspects of plant biology. Functional studies of ubiquitylation have focused on the function of ubiquitylating enzymes, especially the E3 ligases, rather than deubiquitylating enzymes (DUBs) or ubiquitin isopeptidases, enzymes that hydrolyze ubiquitin chains. One reason may be the smaller number of DUBs in comparison to E3 ligases, implying the broader substrate specificities of DUBs and the difficulties to identify the direct targets. Recent studies have revealed that DUBs actively participate in controlling cellular events and play pivotal roles in plant development and growth.
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