Regulation
Precise regulation of PM H+
-ATPase activity is crucial to the plant. Over-expression of the PM H+
-ATPase is compensated by a down-regulation of activity, whereas deletion of an isoform is compensated by redundancy as well as augmented activity of other isoforms by increased level of post-translational modifications. The PM H+
-ATPase is subject to autoinhibition, which negatively regulates the activity of the pump and keeps the enzyme in a low activity state where ATP hydrolytic activity is partly uncoupled from ATP hydrolysis,. Release from the autoinhibitory restraints requires posttranslational modifications such as phosphorylation and interacting proteins. Autoinhibition is achieved by the N- and C-termini of the protein - communication between the two termini facilitates the necessary precise control of pump activity. The autoinhibitory C-terminal domain can be displaced by phosphorylation of the penultimate Thr residue and the subsequent binding of 14-3-3 proteins. The PM H+
-ATPase is the first P-type ATPase for which both termini have been demonstrated to take part in the regulation of protein activity.
Read more about this topic: Proton ATPase
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