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JCS ePress online publication date 15 Aug 2006
doi: 10.1242/jcs.03104

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Research Article

Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III {beta} protects from dephosphorylation and stabilizes lipid kinase activity


Angelika Hausser*, Gisela Link, Miriam Hoene, Chiara Russo, Olaf Selchow, and Klaus Pfizenmaier
* Author for correspondence (e-mail: angelika.hausser{at}izi.uni-stuttgart.de)

Phosphatidylinositol-4-kinase-III{beta} (PI4KIII{beta}) is activated at the Golgi compartment by PKD-mediated phosphorylation. Subsequent mechanisms responsible for continuous PtdIns(4)P production at Golgi membranes and potential interaction partners of activated PI4KIII{beta} are unknown. Here we identify phosphoserine/-threonine binding 14-3-3 proteins as novel regulators of PI4KIII{beta} activity downstream of this phosphorylation. The PI4KIII{beta}-14-3-3 interaction, evident from GST pulldowns, co-immunoprecipitations and bimolecular fluorescence complementation, was augmented by phosphatase inhibition with okadaic acid. Binding of 14-3-3 proteins to PI4KIII{beta} involved the PKD phosphorylation site Ser294, evident from reduced 14-3-3 binding to a S294A PI4KIII{beta} mutant. Expression of dominant negative 14-3-3 proteins resulted in decreased PI4KIII{beta} Ser294 phosphorylation, whereas wildtype 14-3-3 proteins increased phospho-PI4KIII{beta} levels. This was because of protection of PI4KIII{beta} Ser294 phosphorylation from phosphatase-mediated dephosphorylation. The functional significance of the PI4KIII{beta}-14-3-3 interaction was evident from a reduction of PI4KIII{beta} activity upon dominant negative 14-3-3 protein expression. We propose that 14-3-3 proteins function as positive regulators of PI4KIII{beta} activity by protecting the lipid kinase from active site dephosphorylation, thereby ensuring a continuous supply of PtdIns(4)P at the Golgi compartment.
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