Institutional Publications

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Author: search.filters.author.Prasad, ManojSubject: search.filters.subject.E3 ligase

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    Ubiquitination from the perspective of plant pathogens
    (Oxford University Press, 2023) Sharma, Shambhavi; Prasad, Ashish; Prasad, Manoj
    The constant battle of survival between pathogens and host plants has played a crucial role in shaping the course of their co-evolution. However, the major determinants of the outcome of this ongoing arms race are the effectors secreted by pathogens into the host cells. These effectors perturb the defense responses of plants to promote their successful infection. In recent years, the extensive research in the area of effector biology has reported an increase in the repertoire of pathogenic effectors that mimics or targets the conserved ubiquitin proteasomal pathway. The role of ubiquitin mediated degradation pathway has been well known to be indispensable for various aspects of plant’s life, thus targeting or mimicking it seems to be a smart strategy adopted by pathogens in their favor. Therefore, this review summarizes the recent findings on how some pathogenic effectors mimics or act as one of the components of ubiquitin proteasomal machinery while others directly target the plant’s ubiquitin proteasomal system.
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    Ubiquitination: a tool for plant adaptation to changing environments
    (Springer Nature, 2018) Mandal, Arunava; Sharma, Namisha; Muthamilarasan, Mehanathan; Prasad, Manoj
    Post-translational modifcations namely ubiquitination, phosphorylation, methylation and acetylation play distinct roles in regulating the growth and development of plants. Among these, the ubiquitination regulates the abundance, activities, subcellular compartmentalization and trafcking of regulatory proteins involved in diverse developmental as well as stress-responsive processes. The ubiquitin–proteasome system (UPS) involves fve essential components namely ubiquitin, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3) and the intact 26S proteasome. The E3 ubiquitin ligase is the major component of UPS that recognizes and tethers poly-ubiquitins on the target proteins. Owing to its specifcity of substrate recognition, the E3 ubiquitin ligase contributes not only to the proteome plasticity of the cell but also regulates the plant’s response to environmental cues. In this context, the review summarizes the components involved in UPS and elaborates the role of E3 ubiquitin ligase in biotic and abiotic stress responses.