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

Date

2014

Authors

Pottosin, I.
Velarde-Buendia, A.
Bose, J.
Zepeda-Jazo, I.
Shabala, S.
Dobrovinskaya, O.

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Journal article

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Journal of Experimental Botany, 2014; 65(5):1271-1283

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Igor Pottosin, Ana María Velarde-Buendía, Jayakumar Bose, Isaac Zepeda-Jazo, Sergey Shabala and Oxana Dobrovinskaya

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Abstract

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 Ca2+ 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 Ca2+-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 Ca2+-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 Ca2+ signalling.

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First published online: January 24, 2014

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© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology.

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