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Ubiquitin-Proteasome System-Mediated Protein Degradation in Defense Signaling

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Book cover PAMP Signals in Plant Innate Immunity

Part of the book series: Signaling and Communication in Plants ((SIGCOMM,volume 21))

Abstract

Ubiquitin-proteasome system plays important role in the complex PAMP signal transduction systems involved in plant innate immunity. JAZ proteins, which are activated by jasmonate (JA) signals, act as repressors of JA-dependent transcription factors. COI1 protein, a receptor of JA signal, forms a functional E3 ubiquitin ligase and is required for removal of repressors of the JA signaling pathway. Ubiquitin proteins-cullin-RING ligases negatively regulate biosynthesis of ethylene. Ethylene signal transduction terminates in a transcription cascade involving the EIN3/EIL and ERF families of transcription factors and ubiquitin ligases regulate the stability and expression of these transcription factors. Ubiquitin proteasome may positively or negatively regulate SA biosynthesis. A 26S proteosome is involved in triggering SA accumulation, probably by removing/degrading an inhibitor of SA biosynthesis. Ubiquitin ligases are also involved in regulation of R proteins-mediated defense responses. Major function of ubiquitin ligases may be in conferring stability to R proteins, probably by degrading the proteins involved in reducing the stability of R proteins. Small ubiquitin-like modifier (SUMO) plays a significant role in SA-mediated systemic acquired resistance. Ubiquitin-proteasome is involved in triggering defense responses and virulent pathogens may subvert ubiquitin-proteasome system to cause disease.

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  1. Plant Pathology, Tamil Nadu Agricultural University, Coimbatore, Tamil Nadu, India

    P. Vidhyasekaran

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Vidhyasekaran, P. (2014). Ubiquitin-Proteasome System-Mediated Protein Degradation in Defense Signaling. In: PAMP Signals in Plant Innate Immunity. Signaling and Communication in Plants, vol 21. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7426-1_10

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