Abstract
Protein kinase D (PKD) regulates the fission of vesicles originating from the trans-Golgi network1,2. We show that phosphatidylinositol 4-kinase IIIβ (PI4KIIIβ) — a key player in the structure and function of the Golgi complex3 — is a physiological substrate of PKD. Of the three PKD isoforms, only PKD1 and PKD2 phosphorylated PI4KIIIβ at a motif that is highly conserved from yeast to humans. PKD-mediated phosphorylation stimulated lipid kinase activity of PI4KIIIβ and enhanced vesicular stomatitis virus G-protein transport to the plasma membrane. The identification of PI4KIIIβ as one of the PKD substrates should help to reveal the molecular events that enable transport-carrier formation.
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Acknowledgements
We wish to thank L. Rameh for help with the lipid-kinase assay, and E. Behrle and O. Selchow for help with the confocal microscopy. This work was supported by grants from the Deutsche Forschungsgemeinschaft (SFB 495 to K.P.), the Landesstiftung Baden-Württemberg (to A.H.) and from the National Institutes of Health (CA075134 to A.T.).
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Hausser, A., Storz, P., Märtens, S. et al. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIβ at the Golgi complex. Nat Cell Biol 7, 880–886 (2005). https://doi.org/10.1038/ncb1289
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DOI: https://doi.org/10.1038/ncb1289
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