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

HAVLIŠ, Jan and Christine WALCH-SOLIMENA. Nucleo-cytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth. Molecular and Cellular Biology. Washington, D.C.: ASM, 2008, vol. 19, No 3, p. 1046-61, 16 pp. ISSN 0270-7306.

Basic information

• Original name: Nucleo-cytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth
• Authors: HAVLIŠ, Jan and Christine WALCH-SOLIMENA.
• Edition: Molecular and Cellular Biology, Washington, D.C. ASM, 2008, 0270-7306.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: Genetics and molecular biology
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 5.942
• Organization unit: Faculty of Science
• UT WoS: 000258951400024
• Keywords in English: phosphatidylinositol 4-kinase Pik1; Golgi apparatus; 14-3-3 proteins; cell growth
• Tags: 14-3-3 proteins, cell growth, Golgi apparatus, phosphatidylinositol 4-kinase Pik1
• Tags: International impact, Reviewed

Abstract

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.