Nucleo-cytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth

Varování

Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	HAVLIŠ Jan BECK Mike WALCH-SOLIMENA Christine KLOSE Christian SCHLAITZ Anne-Lore GLOOR Yvonne HSU Peggy P. SHEVCHENKO Andrej KRAUSE Eberhard KALAIDZIDIS Yannis
Rok publikování	2008
Druh	Článek v odborném periodiku
Časopis / Zdroj	Molecular and Cellular Biology
Fakulta / Pracoviště MU	Přírodovědecká fakulta
Citace
Obor	Genetika a molekulární biologie
Klíčová slova	phosphatidylinositol 4-kinase Pik1; Golgi apparatus; 14-3-3 proteins; cell growth
Popis	The yeast phosphatidylinositol 4-kinase Pik1p is essential for proliferation, and it 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 nucleocytoplasmic 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 nucleocytoplasmic shuttling in coordination of biosynthetic transport from the Golgi with nutrient signaling.