The Expression of the t-SNARE AtSNAP33 Is Induced by Pathogens and Mechanical Stimulation1
AUTOR(ES)
Wick, Peter
FONTE
American Society of Plant Biologists
RESUMO
The fusion of vesicles in the secretory pathway involves the interaction of t-soluble N-ethylmaleimide-sensitive factor attachment protein receptors (t-SNAREs) on the target membrane and v-SNAREs on the vesicle membrane. AtSNAP33 is an Arabidopsis homolog of the neuronal t-SNARE SNAP-25 involved in exocytosis and is localized at the cell plate and at the plasma membrane. In this paper, the expression of AtSNAP33 was analyzed after different biotic and abiotic stresses. The expression of AtSNAP33 increased after inoculation with the pathogens Plectosporium tabacinum and virulent and avirulent forms of Peronospora parasitica and Pseudomonas syringae pv tomato. The expression of PR1 transcripts encoding the secreted pathogenesis-related protein 1 also increased after inoculation with these pathogens and the expression of AtSNAP33 preceded or occurred at the same time as the expression of PR1. AtSNAP33 was also expressed in npr1 plants that do not express PR1 after pathogen inoculation as well as in cpr1 plants that overexpress PR1 in the absence of a pathogen. The level of AtSNAP33 decreased slightly in leaves inoculated with P. parasitica in the NahG plants, and eds5 and sid2 mutants that are unable to accumulate salicylic acid (SA) after pathogen inoculation, indicating a partial dependence on SA. AtSNAP33 was also expressed in systemic noninoculated leaves of plants inoculated with P. syringae. In contrast to the situation in infected leaves, the expression of AtSNAP33 in systemic leaves was fully SA dependent. Thus, the expression of AtSNAP33 after pathogen attack is regulated by SA-dependent and SA-independent pathways. Mechanical stimulation also led to an increase of AtSNAP33 transcripts.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=166979Documentos Relacionados
- Phosphorylation of SNAP-23 by the Novel Kinase SNAK Regulates t-SNARE Complex Assembly
- t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast
- A Yeast t-SNARE Involved in Endocytosis
- t-SNARE Phosphorylation Regulates Endocytosis in Yeast
- The t-SNARE AtVAM3p Resides on the Prevacuolar Compartment in Arabidopsis Root Cells1