Evidence map›Paper›PMID 18172025›Full record

ArticleMolecular biology of the cell2008

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

Lars Demmel, Mike Beck, Christian Klose, Anne-Lore Schlaitz, Yvonne Gloor, Peggy P Hsu, Jan Havlis, Andrej Shevchenko, Eberhard Krause, Yannis Kalaidzidis and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  8. The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Activation of the CaMolecular biology of the cell · 2019
    Article
  11. Review
  12. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  13. Review
  14. Article
  15. Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Components of the CtBP1/BARS-dependent fission machinery.Histochemistry and cell biology · 2013
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 3 countries.

Lars DemmelMax Planck Institute of Molecular Cell Biology and Genetics, Dresden D-01307, Germany.
Mike Beck
Christian Klose
Anne-Lore Schlaitz
Yvonne Gloor
Peggy P Hsu
Jan Havlis
Andrej Shevchenko
Eberhard Krause
Yannis Kalaidzidis
Christiane Walch-Solimena
Max Planck Institute of Molecular Cell Biology and Genetics · DELeibniz Association · DELomonosov Moscow State University · RUWhitehead Institute for Biomedical Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

14-3-3 Proteins1-Phosphatidylinositol 4-KinaseActive Transport, Cell NucleusAmino Acid SequenceCell NucleusCell ProliferationFoodGolgi ApparatusModels, BiologicalMolecular Sequence DataMultiprotein ComplexesMutationPhosphorylationPhosphoserineProtein BindingSaccharomyces cerevisiae14-3-3 Proteins1-Phosphatidylinositol 4-KinaseMultiprotein ComplexesPhosphoserinePIK1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID18172025
PMCPMC2262966
OpenAlexW2171363796

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.