Evidence map›Paper›PMID 12912920›Full record

ArticleThe EMBO journal2003

Regulation of PI4,5P2 synthesis by nuclear-cytoplasmic shuttling of the Mss4 lipid kinase.

Anjon Audhya, Scott D Emr

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.4field-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

58 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  7. Article
  8. Article
  9. Stage-Specific Genetic Interaction betweenInternational journal of molecular sciences · 2022
    Article
  10. Article
  11. Structure of human BCCIP and implications for binding and modification of partner proteins.Protein science : a publication of the Protein Society · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Analysis of the roles of phosphatidylinositol-4,5-Molecular biology of the cell · 2019
    Article
  16. Article
  17. Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018
    Review
  18. Article
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Anjon AudhyaDepartment of Cellular and Molecular Medicine, University of California, San Diego, School of Medicine, La Jolla, CA 92093-0668, USA.
Scott D Emr
Howard Hughes Medical Institute · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
NCI NIH HHS CA58689
6 · The paper itself

Abstract

The essential phospholipid PI4,5P(2) is generated by a well conserved PI4P 5-kinase, Mss4, in yeast. Balanced production and turnover of PI4,5P(2) is important for normal organization of the actin cytoskeleton and cell viability. Previous studies have shown that multiple PI phosphatases can regulate PI4,5P(2) levels. We report a new, unexpected regulatory mechanism for PI4,5P(2) homeostasis, directed by nuclear-cytoplasmic shuttling of the lipid kinase. We show that Mss4 is a phosphoprotein, which contains a functional nuclear localization signal (NLS) and can shuttle between the cytoplasm and the nucleus. Temperature-conditional mss4 cells that accumulate Mss4 protein in the nucleus exhibit reduced levels of PI4,5P(2), depolarization of the actin cytoskeleton and a block in Mss4 phosphorylation, suggesting an essential role for phosphorylated Mss4 at the plasma membrane. Through the isolation of gene dosage-dependent suppressors of mss4 mutants, we identified Bcp1, a protein enriched in the nucleus, which is required for Mss4 nuclear export and is related to the mammalian BRCA2-interacting protein BCCIP. Together, these studies suggest a new mechanism for lipid kinase regulation through regulated nuclear-cytoplasmic shuttling.

Indexed as

Gene Expression Regulation, EnzymologicPhosphotransferasesActinsBiological Transport, ActiveCasein KinasesCell MembraneCell NucleusCell Transformation, ViralCytoplasmGene DosageGenes, SuppressorModels, BiologicalMutationNuclear Localization SignalsNuclear ProteinsPhosphatidylinositol 4,5-DiphosphateActinsBcp1 protein, S cerevisiaeCasein KinasesMSS4 protein, S cerevisiaeNuclear Localization SignalsNuclear ProteinsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferasesPhosphotransferases (Alcohol Group Acceptor)Protein KinasesProteinsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID12912920
PMCPMC175787
OpenAlexW2062009669

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.