Signalling in guard cells and regulation of ion channel activity

J Exp Bot. 1997 Mar;48 Spec No:515-28. doi: 10.1093/jxb/48.Special_Issue.515.


A review is presented of the properties of ion channels in plasmalemma and tonoplast of stomatal guard cells, their regulation, with particular reference to Ca(2+) and protein phosphorylation/dephosphorylation, and of the evidence for ABA-induced changes in specific ion channels, with an attempt to identify the signalling chains involved in each such change. A key question is whether a local increase in Ca(2+), close to cell membranes and capable of triggering Ca(2+)-dependent changes in a variety of ion channels, is a universal feature of the ABA-reponse. If this is so, then there exist Ca(2+)-coupled mechanisms for most of the observed changes, including inhibition of the inward K(+) channel and activation of the slow anion channel in the plasmalemma, and activation of two channels in the tonoplast, the K(+)-selective (VK) channel and the slow vacuolar (SV) channel, initiating efflux of both anions and cations from the vacuole. The detailed signalling chains are not complete, and the role of protein phosphorylation/dephosphorylation is not clearly defined, nor linked to ABA. Control of the outward K(+) channel is Ca(2+)-independent; its activation by ABA may be mediated by cytoplasmic alkalinization, but the role of protein dephosphorylation in the signalling chain has still to be clarified. If Ca(2+) is not available as second messenger, then the signalling chains involved have hardly begun to be understood. Detailed comparison of the efflux transients in different conditions provides evidence that ABA changes the 'set-point' of a stretch-activated channel, initiating loss of vacuolar K(+). The inclusion of Ba(2+) in the bathing solution has effects similar to those of reduced ABA concentration, a delay in initiating the vacuolar transient, and a slower rise to a reduced peak height. It is suggested that this could be the result of inhibition of the process of Ca(2+) release from internal stores, by blocking a charge-balancing K(+) flux.