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Cross-talk between reactive oxygen species and polyamines in regulation of ion transport across the plasma membrane: implications for plant adaptive responses

期刊

JOURNAL OF EXPERIMENTAL BOTANY
卷 65, 期 5, 页码 1271-1283

出版社

OXFORD UNIV PRESS
DOI: 10.1093/jxb/ert423

关键词

Abiotic stress; amine oxidase; apoplast; calcium; hydroxyl radical; hypersensitive response; ion channel; P-type ATPase; plasma membrane; polyamine; reactive oxygen species; root; stomata

资金

  1. CONACyT
  2. ARC
  3. GRDC
  4. University of Tasmania

向作者/读者索取更多资源

Many stresses are associated with increased accumulation of reactive oxygen species (ROS) and polyamines (PAs). PAs act as ROS scavengers, but export of putrescine and/or PAs to the apoplast and their catabolization by amine oxidases gives rise to H2O2 and other ROS, including hydroxyl radicals (OH). PA catabolization-based signalling in apoplast is implemented in plant development and programmed cell death and in plant responses to a variety of biotic and abiotic stresses. Central to ROS signalling is the induction of Ca-2 influx across the plasma membrane. Different ion conductances may be activated, depending on ROS, plant species, and tissue. Both H2O2 and OH can activate hyperpolarization-activated Ca-2-permeable channels. OH is also able to activate both outward K current and weakly voltage-dependent conductance (ROSIC), with a variable cation-to-anion selectivity and sensitive to a variety of cation and anion channel blockers. Unexpectedly, PAs potentiated OH-induced K efflux in vivo, as well as ROSIC in isolated protoplasts. This synergistic effect is restricted to the mature root zone and is more pronounced in salt-sensitive cultivars compared with salt-tolerant ones. ROS and PAs suppress the activity of some constitutively expressed K and non-selective cation channels. In addition, both OH and PAs activate plasma membrane Ca-2-ATPase and affect H pumping. Overall, OH and PAs may provoke a substantial remodelling of cation and anion conductance at the plasma membrane and affect Ca-2 signalling.

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