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The Plant journal : for cell and molecular biology, 2002-10, Vol.32 (2), p.185-194
2002
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Autor(en) / Beteiligte
Titel
Protein phosphorylation activates the guard cell Ca2+ channel and is a prerequisite for gating by abscisic acid
Ist Teil von
  • The Plant journal : for cell and molecular biology, 2002-10, Vol.32 (2), p.185-194
Ort / Verlag
Oxford, UK: Blackwell Science Ltd
Erscheinungsjahr
2002
Quelle
Wiley Blackwell Single Titles
Beschreibungen/Notizen
  • Summary Protein phosphorylation and cytosolic‐free [Ca2+] ([Ca2+]i) contribute to signalling cascades evoked by the water‐stress hormone abscisic acid (ABA) that lead to stomatal closure in higher‐plant leaves. ABA activates an inward‐rectifying Ca2+ channel at the plasma membrane of stomatal guard cells, promoting Ca2+ entry by shifting the voltage‐sensitivity of the channels. Because many of these effects could be mediated by kinase/phosphatase action at the membrane, we examined a role for protein (de‐)phosphorylation in plasma membrane patches from Vicia guard cells. Ca2+ channel activity decayed rapidly in excised patches, and recovered on adding ATP (K1/2, 1.3 ± 0.7 mm) but not the non‐hydrolyzable analog ATPγS. ABA activation of the channel required the presence of ATP and like ABA, the 1/2 A‐type protein phosphatase antagonists okadaic acid (OA) and calyculin A (CA) enhanced Ca2+ channel activity by increasing the open probability and number of active channels. Neither ATP nor the antagonists affected the mean open lifetime of the channel, suggesting an action through changes in closed lifetime distributions. Like ABA, OA and CA shifted the voltage‐sensitivities of the Ca2+ current and [Ca2+]i increases in intact guard cells towards positive voltages. OA and CA also augmented the [Ca2+]i rise evoked by hyperpolarization and delayed its recovery. These results demonstrate a membrane‐delimited interaction between 1/2 A‐type protein phosphatase(s) and the Ca2+ channel or associated proteins, and they are consistent with a role for protein (de‐)phosphorylation in ABA signalling mediated directly through Ca2+ channel gating that leads to [Ca2+]i increases in the guard cells.

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