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

J 2008

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 a Christine WALCH-SOLIMENA

Základní údaje

Originální název

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

Autoři

HAVLIŠ, Jan a Christine WALCH-SOLIMENA

Vydání

Molecular and Cellular Biology, Washington, D.C. ASM, 2008, 0270-7306

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 5.942

Označené pro přenos do RIV

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000258951400024

Klíčová slova anglicky

phosphatidylinositol 4-kinase Pik1; Golgi apparatus; 14-3-3 proteins; cell growth

Štítky

14-3-3 proteins, cell growth, Golgi apparatus, phosphatidylinositol 4-kinase Pik1

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 2. 7. 2009 18:59, doc. Mgr. Jan Havliš, Dr.

Anotace

V originále

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.

Citovat

HAVLIŠ, Jan a 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, roč. 19, č. 3, s. 1046-61, 16 s. ISSN 0270-7306.

@article{768345,
   author = {Havliš, Jan and WalchandSolimena, Christine},
   article_location = {Washington, D.C.},
   article_number = {3},
   keywords = {phosphatidylinositol 4-kinase Pik1; Golgi apparatus; 14-3-3 proteins; cell growth},
   language = {eng},
   issn = {0270-7306},
   journal = {Molecular and Cellular Biology},
   title = {Nucleo-cytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth},
   volume = {19},
   year = {2008}
}

TY  - JOUR
ID  - 768345
AU  - Havliš, Jan - Walch-Solimena, Christine
PY  - 2008
TI  - Nucleo-cytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth
JF  - Molecular and Cellular Biology
VL  - 19
IS  - 3
SP  - 1046-61
EP  - 1046-61
PB  - ASM
SN  - 02707306
KW  - phosphatidylinositol 4-kinase Pik1
KW  - Golgi apparatus
KW  - 14-3-3 proteins
KW  - cell growth
N2  - 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.
ER  -

HAVLIŠ, Jan a 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. \textit{Molecular and Cellular Biology}. Washington, D.C.: ASM, 2008, roč.~19, č.~3, s.~1046-61, 16 s. ISSN~0270-7306.

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