Ubiquitination is a reversible post-translational modification that orchestrates a wide spectrum of fundamental processes throughout the plant life cycle. Executed by a hierarchical E1-E2-E3 cascades, this modification tags targets with ubiquitin to modulate their turnover, activity, or subcellular compartmentalization. Among the diverse E3 ligase families, plant U-box (PUB) proteins stand out as a prominent class that determines substrate selection and has emerged as a focal point of stress biology. In this review, we first delineate the structural features of PUB proteins, highlighting their conserved domains and associated regulatory motifs. We then systematically dissect their multifaceted functions in abiotic stress adaptation, encompassing drought, salinity, extreme temperatures, oxidative stress, heavy metal toxicity, with particular emphasis on their integration with ABA signaling networks. We further outline critical knowledge gaps and propose future strategies to decode the regulatory architecture of PUBs. Collectively, this review provides a theoretical foundation and new insights for facilitating the genetic improvement of crop resilience in the face of continuously intensifying environmental stresses through the manipulation of PUB-mediated ubiquitination networks.
Yu-Jie Fang, Han Wu, Yu-Han Wang et al.· Plant Science· 0 citations
The results show that different strains have divergent activation patterns of immune genes and may adopt distinct colonization modes, which provide an important basis for selecting Agrobacterium strains for transient expression in N. benthamiana, optimizing tobacco transient expression systems, and constructing high-efficiency plant bioreactors.
Tairu Wu, Weisong Pan, Wai-Chin Li et al.· Frontiers in Plant Science· 0 citations
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