Changes in actin dynamics are involved in salicylic acid signaling pathway
Jazyk angličtina Země Irsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
24767113
DOI
10.1016/j.plantsci.2014.03.002
PII: S0168-9452(14)00046-6
Knihovny.cz E-zdroje
- Klíčová slova
- Actin dynamics, PR genes, Phosphatidic acid, Salicylic acid,
- MeSH
- aktiny metabolismus MeSH
- Arabidopsis cytologie účinky léků genetika metabolismus MeSH
- cyklopentany metabolismus MeSH
- epidermis rostlin cytologie účinky léků metabolismus MeSH
- kyselina salicylová metabolismus farmakologie MeSH
- kyseliny fosfatidové farmakologie MeSH
- mikrofilamenta účinky léků metabolismus MeSH
- oxylipiny metabolismus MeSH
- proudění cytoplazmy účinky léků MeSH
- regulace genové exprese u rostlin účinky léků MeSH
- signální transdukce * účinky léků genetika MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aktiny MeSH
- cyklopentany MeSH
- jasmonic acid MeSH Prohlížeč
- kyselina salicylová MeSH
- kyseliny fosfatidové MeSH
- oxylipiny MeSH
Changes in actin cytoskeleton dynamics are one of the crucial players in many physiological as well as non-physiological processes in plant cells. Positioning of actin filament arrays is necessary for successful establishment of primary lines of defense toward pathogen attack, depolymerization leads very often to the enhanced susceptibility to the invading pathogen. On the other hand it was also shown that the disruption of actin cytoskeleton leads to the induction of defense response leading to the expression of PATHOGENESIS RELATED proteins (PR). In this study we show that pharmacological actin depolymerization leads to the specific induction of genes in salicylic acid pathway but not that involved in jasmonic acid signaling. Life imaging of leafs of Arabidopsis thaliana with GFP-tagged fimbrin (GFP-fABD2) treated with 1 mM salicylic acid revealed rapid disruption of actin filaments resembling the pattern viewed after treatment with 200 nM latrunculin B. The effect of salicylic acid on actin filament fragmentation was prevented by exogenous addition of phosphatidic acid, which binds to the capping protein and thus promotes actin polymerization. The quantitative evaluation of actin filament dynamics is also presented.
Citace poskytuje Crossref.org
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