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MBC in Press, published online ahead of print January 2, 2008
Mol. Biol. Cell 10.1091/mbc.E07-02-0134

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Submitted on February 16, 2007
Revised on December 13, 2007
Accepted on December 20, 2007

Nucleo-cytoplasmic Shuttling of the Golgi Phosphatidylinositol 4-Kinase Pik1 Is Regulated by 14-3-3 Proteins and Coordinates Golgi Function with Cell Growth

Lars Demmel,*{dagger} Mike Beck,*{dagger} Christian Klose,{dagger} Anne-Lore Schlaitz,{dagger} Yvonne Gloor,{dagger} Peggy P. Hsu,{ddagger} Jan Havlis,{dagger}{sect} Andrej Shevchenko,{dagger} Eberhard Krause,|| Yannis Kalaidzidis,{dagger} and Christiane Walch-Solimena{dagger}

{dagger}Max Planck Institute of Molecular Cell Biology and Genetics, Dresden D-01307, Germany; {ddagger}Whitehead Institute for Biomedical Research, Cambridge, MA 02142; ||Mass Spectrometry Group, Leibniz Institute of Molecular Pharmacology, Berlin D-13125, Germany; A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia

Monitoring Editor: Benjamin Glick

The yeast phosphatidylinositol 4-kinase Pik1p is essential for proliferation and controls Golgi homeostasis and transport of newly synthesized proteins from this compartment. At the Golgi, phosphatidylinositol 4-phosphate recruits multiple cytosolic effectors involved in formation of post-Golgi transport vesicles. A second pool of catalytically active Pik1p localizes to the nucleus. The physiological significance and regulation of this dual localization of the lipid kinase remains unknown. Here we show that Pik1p binds to the redundant 14–3-3 proteins Bmh1p and Bmh2p. We provide evidence that nucleo-cytoplasmic shuttling of Pik1p involves phosphorylation and that 14–3-3 proteins bind Pik1p in the cytoplasm. Nutrient deprivation results in relocation of Pik1p from the Golgi to the nucleus and increases the amount of Pik1p - 14–3-3 complex, a process reversed upon restored nutrient supply. These data suggest a role of Pik1p nucleo-cytoplasmic shuttling in coordination of biosynthetic transport from the Golgi with nutrient signaling.

*These authors contributed equally to this work.

{sect}Present address: Faculty of Science, Department of Analytical Chemistry, Masaryk University, Brno, Czech Republic.

Address correspondence to: Christiane Walch-Solimena (csolimena{at}mpi-cbg.de)




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