The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity
Plants possess a sophisticated immune system to recognize and respond to microbial threats in their environment. The level of immune signaling must be tightly regulated so that immune responses can be quickly activated in the presence of pathogens, while avoiding autoimmunity. HSP90s, along with the...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-03-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00309/full |
| _version_ | 1819266832190668800 |
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| author | Xin eLi Charles eCopeland Kevin eAo Meixuezi eTong YAN eHUANG |
| author_facet | Xin eLi Charles eCopeland Kevin eAo Meixuezi eTong YAN eHUANG |
| author_sort | Xin eLi |
| collection | DOAJ |
| description | Plants possess a sophisticated immune system to recognize and respond to microbial threats in their environment. The level of immune signaling must be tightly regulated so that immune responses can be quickly activated in the presence of pathogens, while avoiding autoimmunity. HSP90s, along with their diverse array of co-chaperones, forms chaperone complexes that have been shown to play both positive and negative roles in regulating the accumulation of immune receptors and regulators. In this study, we examined the role of AtCHIP, an evolutionarily conserved E3 ligase that was known to interact with chaperones including HSP90s in multicellular organisms including fruit fly, C. elegans, plants and human. Atchip knockout mutants display enhanced disease susceptibility to a virulent oomycete pathogen, and overexpression of AtCHIP causes enhanced disease resistance at low temperature. Although CHIP was reported to target HSP90 for ubiquitination and degradation, accumulation of HSP90.3 was not affected in Atchip plants. In addition, protein accumulation of nucleotide-binding, leucine-rich repeat domain immune receptor (NLR) SNC1 is not altered in Atchip mutant. Thus, while AtCHIP plays a role in immunity, it does not seem to regulate the turnover of HSP90 or SNC1. Further investigation is needed in order to determine the exact mechanism behind AtCHIP’s role in regulating plant immune responses. |
| first_indexed | 2024-12-23T21:07:32Z |
| format | Article |
| id | doaj.art-1e80819a3a864e62b6211696e3330396 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-23T21:07:32Z |
| publishDate | 2016-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-1e80819a3a864e62b6211696e33303962022-12-21T17:31:10ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-03-01710.3389/fpls.2016.00309172905The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunityXin eLi0Charles eCopeland1Kevin eAo2Meixuezi eTong3YAN eHUANG4University of British ColumbiaUniversity of British ColumbiaUniversity of British ColumbiaUniversity of British ColumbiaUniversity of British ColumbiaPlants possess a sophisticated immune system to recognize and respond to microbial threats in their environment. The level of immune signaling must be tightly regulated so that immune responses can be quickly activated in the presence of pathogens, while avoiding autoimmunity. HSP90s, along with their diverse array of co-chaperones, forms chaperone complexes that have been shown to play both positive and negative roles in regulating the accumulation of immune receptors and regulators. In this study, we examined the role of AtCHIP, an evolutionarily conserved E3 ligase that was known to interact with chaperones including HSP90s in multicellular organisms including fruit fly, C. elegans, plants and human. Atchip knockout mutants display enhanced disease susceptibility to a virulent oomycete pathogen, and overexpression of AtCHIP causes enhanced disease resistance at low temperature. Although CHIP was reported to target HSP90 for ubiquitination and degradation, accumulation of HSP90.3 was not affected in Atchip plants. In addition, protein accumulation of nucleotide-binding, leucine-rich repeat domain immune receptor (NLR) SNC1 is not altered in Atchip mutant. Thus, while AtCHIP plays a role in immunity, it does not seem to regulate the turnover of HSP90 or SNC1. Further investigation is needed in order to determine the exact mechanism behind AtCHIP’s role in regulating plant immune responses.http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00309/fullHSP90 Heat-Shock ProteinsPlant ImmunitychaperonesChIPSGT1E3 lligase |
| spellingShingle | Xin eLi Charles eCopeland Kevin eAo Meixuezi eTong YAN eHUANG The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity Frontiers in Plant Science HSP90 Heat-Shock Proteins Plant Immunity chaperones ChIP SGT1 E3 lligase |
| title | The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity |
| title_full | The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity |
| title_fullStr | The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity |
| title_full_unstemmed | The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity |
| title_short | The evolutionarily conserved E3 ubiquitin ligase AtCHIP contributes to plant immunity |
| title_sort | evolutionarily conserved e3 ubiquitin ligase atchip contributes to plant immunity |
| topic | HSP90 Heat-Shock Proteins Plant Immunity chaperones ChIP SGT1 E3 lligase |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2016.00309/full |
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