Evidence map›Paper›PMID 7663021›Full record

ArticleMolecular biology of the cell1995

Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast.

A Yamamoto, D B DeWald, I V Boronenkov, R A Anderson, S D Emr, D Koshland

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

128 citing papers in PubMed, 278 citations in OpenAlex.

  1. Quantitative comparison of PI(3,5)PMolecular biology of the cell · 2026
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  3. Quantitative comparison of PI(3,5)PbioRxiv : the preprint server for biology · 2025
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  10. Review
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  12. The signalling lipid PI3,5POpen biology · 2023
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  13. Article
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  15. Article
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  17. Yeast cells actively tune their membranes to phase separate at temperatures that scale with growth temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Review

68 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

A YamamotoCarnegie Institution of Washington, Department of Embryology, Baltimore, Maryland 21210, USA.
D B DeWald
I V Boronenkov
R A Anderson
S D Emr
D Koshland
Carnegie Institution for Science · US

Funding

PHOSPHOINOSITIDE SIGNALING TO AND WITHIN THE NUCLEUSR01GM051968 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ANDERSON, RICHARD A. · 1995 to 2012
$3.2M
CASEIN KINASE I REGULATION BY PI-4,5-P2R01GM038906 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI ANDERSEN, RICHARD A · 1992 to 1995
–
MITOTIC CHROMOSOME STRUCTURE IN BUDDING YEASTR01GM041718 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI KOSHLAND, DOUGLAS E. · 1991 to 1999
–
PHOSPHOINOSITIDE REGULATION OF ERYTHROCYTE CYTOSKELETONR29GM038906 · NIGMS · UNIVERSITY OF WISCONSIN MADISON · PI ANDERSEN, RICHARD A · 1987 to 1991
–
NIGMS NIH HHS GM-38906NIGMS NIH HHS GM-41718NIGMS NIH HHS GM-51968
6 · The paper itself

Abstract

The FAB1 gene of budding yeast is predicted to encode a protein of 257 kDa that exhibits significant sequence homology to a human type II PI(4)P 5-kinase (PIP5K-II). The recently cloned human PIP5K-II specifically converts PI(4)P to PI(4,5)P2 (Boronenkov and Anderson, 1995). The region of highest similarity between Fab1p and PIP5K-II includes a predicted nucleotide binding motif, which is likely to correspond to the catalytic domain of the protein. Interestingly, neither PIP5K-II nor Fab1p exhibit significant homology with cloned PI 3-kinases or PI 4-kinases. fab1 mutations result in the formation of aploid and binucleate cells (hence the name FAB). In addition, loss of Fab1p function causes defects in vacuole function and morphology, cell surface integrity, and cell growth. Experiments with a temperature conditional fab1 mutant revealed that their vacuoles rapidly (within 30 min) enlarge to more than double the size upon shifting cells to the nonpermissive temperature. Additional experiments with the fab1 ts mutant together with results obtained with fab1 vps (vacuolar protein sorting defective) double mutants indicate that the nuclear division and cell surface integrity defects observed in fab1 mutants are secondary to the vacuole morphology defects. Based on these data, we propose that Fab1p is a PI(4)P 5-kinase and that the product of the Fab1p reaction, PIP2, functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole. Furthermore, a comparison of the phenotypes of fab1 mutants and other yeast mutants affecting PI metabolism suggests that phosphoinositides may serve as general regulators of several different membrane trafficking pathways.

Indexed as

Saccharomyces cerevisiae ProteinsSequence Homology, Amino AcidAmino Acid SequenceAneuploidyCarboxypeptidasesCathepsin ACell NucleusChromosomes, FungalCloning, MolecularFungal ProteinsGenes, FungalHumansMolecular Sequence DataPhosphotransferases (Alcohol Group Acceptor)Saccharomyces cerevisiaeSequence Analysis, DNA1-phosphatidylinositol-4-phosphate 5-kinaseCarboxypeptidasesCathepsin ACTSA protein, humanFAB1 protein, S cerevisiaeFungal ProteinsPhosphotransferases (Alcohol Group Acceptor)Saccharomyces cerevisiae Proteins

Identifiers

PMID7663021
PMCPMC301213
OpenAlexW2075171680

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.