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The **plasma membrane H+-ATPase–14-3-3 protein complex** in plants consists of a proton pump (plasma membrane H+-ATPase) that is activated when a regulatory 14-3-3 protein binds to its phosphorylated C-terminus. This interaction is crucial for generating the electrochemical gradient across the plasma membrane, which drives nutrient uptake, cell expansion, and turgor maintenance. The active complex can form higher-order oligomers (hexamers), with stoichiometry of six ATPase and six 14-3-3 proteins. The small molecule fusicoccin can lock this complex in an activated state by stabilizing the interaction, making it a classic model for studying regulation of membrane pumps in plants but not a therapeutic target in humans
Activation of plasma membrane H+-ATPase by phosphorylation-dependent binding of 14-3-3 proteins, which stabilize the active conformation and boost ATPase activity Fusicoccin mimics this regulatory mechanism by inducing/stabilizing the complex, resulting in constitutive activation
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