Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus

Strahl, Thomas; Hama, Hiroko; DeWald, Daryll B.; Thorner, Jeremy

doi:10.1083/jcb.200504104

Cited by 122 publications

(171 citation statements)

References 74 publications

(101 reference statements)

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“…The only currently known binding partner of Pik1p is the calmodulin-like protein frequenin-1 (Frq1p), which functions in binding of Pik1p to the Golgi (Hendricks et al, 1999;Ames et al, 2000;Strahl et al, 2005). We now report that Pik1p binds to the yeast 14-3-3 proteins Bmh1p and Bmh2p.…”

Section: Introductionmentioning

confidence: 95%

“…Pik1p has been found at the TGN and in the nucleus (WalchSolimena and Novick, 1999;Sciorra et al, 2005;Strahl et al, 2005). 14-3-3 proteins have a more widespread distribution.…”

Section: Pik1p-14-3-3 Interaction Occurs In the Cytoplasmmentioning

confidence: 99%

“…The phosphatidylinositol 4-kinases (PI 4-kinase) Pik1p in yeast and PI 4-kinase III␤ in vertebrates are found at the trans-Golgi network (TGN) (Godi et al, 1999;Walch-Solimena and Novick, 1999;Sciorra et al, 2005;Strahl et al, 2005), and they are key regulators of membrane transport and Golgi homeostasis. Mutants with defects in PI(4)P production by these lipid kinases showed reduced secretion, delayed vacuolar transport, defective protein retrieval from endosomes to the Golgi, and aberrant Golgi morphology (Godi et al, 1999;Hama et al, 1999;Walch-Solimena and Novick, 1999;Audhya et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…In addition to their TGN localization, both Pik1p and PI 4-kinase III␤ also localize to the nucleus (Garcia-Bustos et al, 1994;Walch-Solimena and Novick, 1999;de Graaf et al, 2002;Strahl et al, 2005). Although the nuclear function of the two PI 4-kinases remains unknown, it has been demonstrated that they undergo nucleocytoplasmic shuttling (de Graaf et al, 2002;Strahl et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…Although the nuclear function of the two PI 4-kinases remains unknown, it has been demonstrated that they undergo nucleocytoplasmic shuttling (de Graaf et al, 2002;Strahl et al, 2005). Reversible relocation of Pik1p from the nucleus to the cytoplasm has been observed upon block of secretion in several sec (secretion) mutants as part of the so-called "arrest of secretion response" (ASR) (WalchSolimena and Novick, 1999;Nanduri and Tartakoff, 2001).…”

Section: Introductionmentioning

confidence: 99%

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

Demmel

Beck

Klose

et al. 2008

MBoC

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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.

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Section: Introductionmentioning

confidence: 95%

“…Pik1p has been found at the TGN and in the nucleus (WalchSolimena and Novick, 1999;Sciorra et al, 2005;Strahl et al, 2005). 14-3-3 proteins have a more widespread distribution.…”

Section: Pik1p-14-3-3 Interaction Occurs In the Cytoplasmmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

Demmel

Beck

Klose

et al. 2008

MBoC

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Phosphatidylinositol‐4‐phosphate: The Golgi and beyond

2013

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Initially identified as a key phosphoinositide that controls membrane trafficking at the Golgi complex, phosphatidylinositol-4-phosphate (PI4P) has emerged as a key molecule in the regulation of a diverse array of cellular functions. In this review we will discuss selected examples of the findings that in the last few years have significantly increased our awareness of the regulation and roles of PI4P in the Golgi complex and beyond. We will also highlight the role of PI4P in infection and cancer. We believe that, with the increasing number of regulators and effectors of PI4P identified, the time is ripe for a more integrated approach of study. A first step in this direction is the delineation of PI4P-centered molecular networks that we provide using data from low and high throughput studies in yeast and mammals.

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Septin‐associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae

Perez

Thorner

2018

Cytoskeleton

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In budding yeast, a collar of septin filaments at the neck between a mother cell and its bud marks the incipient site for cell division and serves as a scaffold that recruits proteins required for proper spatial and temporal execution of cytokinesis. A set of interacting proteins that localize at or near the bud neck, including Aim44/Gps1, Nba1 and Nis1, also has been implicated in preventing Cdc42‐dependent bud site re‐establishment at the division site. We found that, at their endogenous level, Aim44 and Nis1 robustly localize sequentially at the septin collar. Strikingly, however, when overproduced, both proteins shift their subcellular distribution predominantly to the nucleus. Aim44 localizes with the inner nuclear envelope, as well as at the plasma membrane, whereas Nis1 accumulates within the nucleus, indicating that these proteins normally undergo nucleocytoplasmic shuttling. Of the 14 yeast karyopherins, Kap123/Yrb4 is the primary importin for Aim44, whereas several importins mediate Nis1 nuclear entry. Conversely, Kap124/Xpo1/Crm1 is the primary exportin for Nis1, whereas both Xpo1 and Cse1/Kap109 likely contribute to Aim44 nuclear export. Even when endogenously expressed, Nis1 accumulates in the nucleus when Nba1 is absent. When either Aim44 or Nis1 are overexpressed, Nba1 is displaced from the bud neck, further consistent with the mutual interactions of these proteins. Collectively, our results indicate that a previously unappreciated level at which localization of septin‐associated proteins is controlled is via regulation of their nucleocytoplasmic shuttling, which places constraints on their availability for complex formation with other partners at the bud neck.

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Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus

Cited by 122 publications

References 74 publications

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

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

Phosphatidylinositol‐4‐phosphate: The Golgi and beyond

Septin‐associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae

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