Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Abstract

Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

Rice RING protein OsBBI1 with E3 ligase activity confers broad-spectrum resistance against Magnaporthe oryzae by modifying the cell wall defence

“…It starts with the ubiquitination of substrate proteins, which are then targeted for degradation (for review see [27]). Emerging experimental evidence indicates that protein degradation via the Ubi/26S proteasome system plays important roles in plant innate immune response (for review see [28]). …”

Seven in Absentia Proteins Affect Plant Growth and Nodulation inMedicago truncatula

“…Ubiquitination of regulatory proteins plays an important role in plant development and responses to the environment (Ellis et al, 2002;Devoto et al, 2003;Hare et al, 2003;Zeng et al, 2006). Polyubiquitination is mediated by repeated sequential action of three enzymes that activate (E1), conjugate (E2), and finally ligate (E3) ubiquitin (Ub) to target proteins that are subsequently degraded via the 26S proteasome (Glickman and Ciechanover, 2002).…”

Identifying Candidate Genes Based on Linked Markers for Brown Planthopper [Nilaparvata lugens (Stål)] Resistance in Rice (Oryza sativa L.)

“…The details of the major candidate genes identified and their frequency are furnished in Table 2. (Zeng et al, 2006). It was found genes responsible for these processes for example, protein kinases, glycosyltransferases and as well as ubiquitination related genes were noticed.…”