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Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling
We describe a signaling pathway that mediates salt stress responses in Arabidopsis. The response is mechanistically related to endoplasmic reticulum (ER) stress responses described in mammalian systems. Such responses involve processing and relocation to the nucleus of ER membrane-associated transcr...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2156172/ https://www.ncbi.nlm.nih.gov/pubmed/17662035 http://dx.doi.org/10.1111/j.1365-313X.2007.03195.x |
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author | Liu, Jian-Xiang Srivastava, Renu Che, Ping Howell, Stephen H |
author_facet | Liu, Jian-Xiang Srivastava, Renu Che, Ping Howell, Stephen H |
author_sort | Liu, Jian-Xiang |
collection | PubMed |
description | We describe a signaling pathway that mediates salt stress responses in Arabidopsis. The response is mechanistically related to endoplasmic reticulum (ER) stress responses described in mammalian systems. Such responses involve processing and relocation to the nucleus of ER membrane-associated transcription factors to activate stress response genes. The salt stress response in Arabidopsis requires a subtilisin-like serine protease (AtS1P), related to mammalian S1P and a membrane-localized b-ZIP transcription factor, AtbZIP17, a predicted type-II membrane protein with a canonical S1P cleavage site on its lumen-facing side and a b-ZIP domain on its cytoplasmic side. In response to salt stress, it was found that myc-tagged AtbZIP17 was cleaved in an AtS1P-dependent process. To show that AtS1P directly targets AtbZIP17, cleavage was also demonstrated in an in vitro pull-down assay with agarose bead-immobilized AtS1P. Under salt stress conditions, the N-terminal fragment of AtbZIP17 tagged with GFP was translocated to the nucleus. The N-terminal fragment bearing the bZIP DNA binding domain was also found to possess transcriptional activity that functions in yeast. In Arabidopsis, AtbZIP17 activation directly or indirectly upregulated the expression of several salt stress response genes, including the homeodomain transcription factor ATHB-7. Upregulation of these genes by salt stress was blocked by T-DNA insertion mutations in AtS1P and AtbZIP17. Thus, salt stress induces a signaling cascade involving the processing of AtbZIP17, its translocation to the nucleus and the upregulation of salt stress genes. |
format | Text |
id | pubmed-2156172 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-21561722008-01-03 Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling Liu, Jian-Xiang Srivastava, Renu Che, Ping Howell, Stephen H Plant J Original Articles We describe a signaling pathway that mediates salt stress responses in Arabidopsis. The response is mechanistically related to endoplasmic reticulum (ER) stress responses described in mammalian systems. Such responses involve processing and relocation to the nucleus of ER membrane-associated transcription factors to activate stress response genes. The salt stress response in Arabidopsis requires a subtilisin-like serine protease (AtS1P), related to mammalian S1P and a membrane-localized b-ZIP transcription factor, AtbZIP17, a predicted type-II membrane protein with a canonical S1P cleavage site on its lumen-facing side and a b-ZIP domain on its cytoplasmic side. In response to salt stress, it was found that myc-tagged AtbZIP17 was cleaved in an AtS1P-dependent process. To show that AtS1P directly targets AtbZIP17, cleavage was also demonstrated in an in vitro pull-down assay with agarose bead-immobilized AtS1P. Under salt stress conditions, the N-terminal fragment of AtbZIP17 tagged with GFP was translocated to the nucleus. The N-terminal fragment bearing the bZIP DNA binding domain was also found to possess transcriptional activity that functions in yeast. In Arabidopsis, AtbZIP17 activation directly or indirectly upregulated the expression of several salt stress response genes, including the homeodomain transcription factor ATHB-7. Upregulation of these genes by salt stress was blocked by T-DNA insertion mutations in AtS1P and AtbZIP17. Thus, salt stress induces a signaling cascade involving the processing of AtbZIP17, its translocation to the nucleus and the upregulation of salt stress genes. Blackwell Publishing Ltd 2007-09 /pmc/articles/PMC2156172/ /pubmed/17662035 http://dx.doi.org/10.1111/j.1365-313X.2007.03195.x Text en © 2007 The Authors Journal compilation © 2007 Blackwell Publishing Ltd |
spellingShingle | Original Articles Liu, Jian-Xiang Srivastava, Renu Che, Ping Howell, Stephen H Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title | Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title_full | Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title_fullStr | Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title_full_unstemmed | Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title_short | Salt stress responses in Arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
title_sort | salt stress responses in arabidopsis utilize a signal transduction pathway related to endoplasmic reticulum stress signaling |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2156172/ https://www.ncbi.nlm.nih.gov/pubmed/17662035 http://dx.doi.org/10.1111/j.1365-313X.2007.03195.x |
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