期刊
FRONTIERS IN PLANT SCIENCE
卷 6, 期 -, 页码 -出版社
FRONTIERS RESEARCH FOUNDATION
DOI: 10.3389/fpls.2015.00154
关键词
Cullin-RING ligase (CRL); ubiquitin ligase; salicylic acid (SA); NPR1; plant immunity; proteasome; transcription activator; gene expression
资金
- Biotechnology and Biological Sciences Research Council (BBSRC)
- BBSRC [BB/L006219/1]
- Royal Society University [UF090321]
- BBSRC [BB/L006219/1] Funding Source: UKRI
- Royal Society [UF090321] Funding Source: Royal Society
- Biotechnology and Biological Sciences Research Council [1064560, BB/L006219/1] Funding Source: researchfish
Plant immune responses against biotrophic pathogens are regulated by the signaling hormone salicylic acid (SA). SA establishes immunity by regulating a variety of cellular processes, including programmed cell death (POD) to isolate and kill invading pathogens, and development of systemic acquired resistance (SAR) which provides long-lasting, broad-spectrum resistance throughout the plant. Central to these processes is post-translational modification of SA-regulated signaling proteins by ubiquitination, i.e., the covalent addition of small ubiquitin proteins. Emerging evidence indicates SA-induced protein ubiquitination is largely orchestrated by Cullin-RING ligases (CRLs), which recruit specific substrates for ubiquitination using interchangeable adaptors. Ligation of ubiquitin chains interlinked at lysine 48 leads to substrate degradation by the 26S proteasome. Here we discuss how CRL-mediated degradation of both nucleotide-binding/leucine-rich repeat domain containing immune receptors and SA-induced transcription regulators are critical for functional POD and SAR responses, respectively. By placing these recent findings in context of knowledge gained in other eukaryotic model species, we highlight potential alternative roles for processive ubiquitination in regulating the activity of SA mediated immune responses.
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