%0 Journal Article %1 Hausser2006 %A Hausser, Angelika %A Link, Gisela %A Hoene, Miriam %A Russo, Chiara %A Selchow, Olaf %A Pfizenmaier, Klaus %D 2006 %J Journal of Cell Science %K 2006 hausser izi pfizenmaier %N 17 %P 3613--3621 %R 10.1242/jcs.03104 %T Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III β protects from dephosphorylation and stabilizes lipid kinase activity %U https://journals.biologists.com/jcs/article/119/17/3613/29160/Phospho-specific-binding-of-14-3-3-proteins-to %V 119 %X Phosphatidylinositol-4-kinase-IIIbeta (PI4KIIIbeta) 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 PI4KIIIbeta are unknown. Here we identify phosphoserine/-threonine binding 14-3-3 proteins as novel regulators of PI4KIIIbeta activity downstream of this phosphorylation. The PI4KIIIbeta-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 PI4KIIIbeta involved the PKD phosphorylation site Ser294, evident from reduced 14-3-3 binding to a S294A PI4KIIIbeta mutant. Expression of dominant negative 14-3-3 proteins resulted in decreased PI4KIIIbeta Ser294 phosphorylation, whereas wildtype 14-3-3 proteins increased phospho-PI4KIIIbeta levels. This was because of protection of PI4KIIIbeta Ser294 phosphorylation from phosphatase-mediated dephosphorylation. The functional significance of the PI4KIIIbeta-14-3-3 interaction was evident from a reduction of PI4KIIIbeta activity upon dominant negative 14-3-3 protein expression. We propose that 14-3-3 proteins function as positive regulators of PI4KIIIbeta activity by protecting the lipid kinase from active site dephosphorylation, thereby ensuring a continuous supply of PtdIns(4)P at the Golgi compartment. %Z Hausser, AngelikaLink, GiselaHoene, MiriamRusso, ChiaraSelchow, OlafPfizenmaier, KlausengResearch Support, Non-U.S. Gov'tEnglandJ Cell Sci. 2006 Sep 1;119(Pt 17):3613-21. doi: 10.1242/jcs.03104. Epub 2006 Aug 15. %7 2006/08/17 %@ 0021-9533

@article{Hausser2006, abstract = {Phosphatidylinositol-4-kinase-IIIbeta (PI4KIIIbeta) 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 PI4KIIIbeta are unknown. Here we identify phosphoserine/-threonine binding 14-3-3 proteins as novel regulators of PI4KIIIbeta activity downstream of this phosphorylation. The PI4KIIIbeta-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 PI4KIIIbeta involved the PKD phosphorylation site Ser294, evident from reduced 14-3-3 binding to a S294A PI4KIIIbeta mutant. Expression of dominant negative 14-3-3 proteins resulted in decreased PI4KIIIbeta Ser294 phosphorylation, whereas wildtype 14-3-3 proteins increased phospho-PI4KIIIbeta levels. This was because of protection of PI4KIIIbeta Ser294 phosphorylation from phosphatase-mediated dephosphorylation. The functional significance of the PI4KIIIbeta-14-3-3 interaction was evident from a reduction of PI4KIIIbeta activity upon dominant negative 14-3-3 protein expression. We propose that 14-3-3 proteins function as positive regulators of PI4KIIIbeta activity by protecting the lipid kinase from active site dephosphorylation, thereby ensuring a continuous supply of PtdIns(4)P at the Golgi compartment.}, added-at = {2018-02-01T15:46:11.000+0100}, annote = {Hausser, AngelikaLink, GiselaHoene, MiriamRusso, ChiaraSelchow, OlafPfizenmaier, KlausengResearch Support, Non-U.S. Gov'tEnglandJ Cell Sci. 2006 Sep 1;119(Pt 17):3613-21. doi: 10.1242/jcs.03104. Epub 2006 Aug 15.}, author = {Hausser, Angelika and Link, Gisela and Hoene, Miriam and Russo, Chiara and Selchow, Olaf and Pfizenmaier, Klaus}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/23713eecc20971272e3f37992f25c290d/cristiano}, doi = {10.1242/jcs.03104}, edition = {2006/08/17}, interhash = {48827f6bc17d3864483ffeee9a882332}, intrahash = {3713eecc20971272e3f37992f25c290d}, isbn = {0021-9533}, issn = {0021-9533}, journal = {Journal of Cell Science}, keywords = {2006 hausser izi pfizenmaier}, number = 17, pages = {3613--3621}, pmid = {16912074}, timestamp = {2023-06-02T12:29:23.000+0200}, title = {{Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III β protects from dephosphorylation and stabilizes lipid kinase activity}}, url = {https://journals.biologists.com/jcs/article/119/17/3613/29160/Phospho-specific-binding-of-14-3-3-proteins-to}, volume = 119, year = 2006 }