Evidence map›Paper›PMID 9693364›Full record

ArticleMolecular biology of the cell1998

ADP-Ribosylation factors do not activate yeast phospholipase Ds but are required for sporulation.

S A Rudge, M M Cavenagh, R Kamath, V A Sciorra, A J Morris, R A Kahn, J Engebrecht

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

18 citing papers in PubMed, 49 citations in OpenAlex.

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  17. ADP-ribosylation factor and phosphatidic acid levels in Golgi membranes during budding of coatomer-coated vesicles.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  18. Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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

7 authors at 2 institutions in 1 country.

S A RudgeDepartment of Pharmacological Sciences, State University of New York, Stony Brook, New York 11794-8651, USA.
M M Cavenagh
R Kamath
V A Sciorra
A J Morris
R A Kahn
J Engebrecht
State University of New York · USEmory University · US

Funding

Role of Lipid Phosphatases in Cholesterol and Triglyceride SynthesisR01GM050388 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI MORRIS, ANDREW J · 1994 to 2011
$2.7M
GENETIC ANALYSIS OF MEIOTIC CHROMOSOME SEGREGATIONR29GM048639 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI ENGEBRECHT, JOANNE · 1993 to 1998
–
REGULATION OF PHOSPHOLIPASE DR55GM054641 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI MORRIS, ANDREW J · 1996 to 1996
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NIGMS NIH HHS GM4863903NIGMS NIH HHS GM50388NIGMS NIH HHS GM54641NIGMS NIH HHS R01 GM050388
6 · The paper itself

Abstract

ADP-ribosylation factor (ARF) proteins in Saccharomyces cerevisiae are encoded by two genes, ARF1 and ARF2. The addition of the c-myc epitope at the C terminus of Arf1 resulted in a mutant (arf1-myc arf2) that supported vegetative growth and rescued cells from supersensitivity to fluoride, but homozygous diploids failed to sporulate. arf1-myc arf2 mutants completed both meiotic divisions but were unable to form spores. The SPO14 gene encodes a phospholipase D (PLD), whose activity is essential for mediating the formation of the prospore membrane, a prerequisite event for spore formation. Spo14 localized normally to the developing prospore membrane in arf1-myc arf2 mutants; however, the synthesis of the membrane was attenuated. This was not a consequence of reduced PLD catalytic activity, because the enzymatic activity of Spo14 was unaffected in meiotic arf1-myc arf2 mutants. Although potent activators of mammalian PLD1, Arf1 proteins did not influence the catalytic activities of either Spo14 or ScPld2, a second yeast PLD. These results demonstrate that ARF1 is required for sporulation, and the mitotic and meiotic functions of Arf proteins are not mediated by the activation of any known yeast PLD activities. The implications of these results are discussed with respect to current models of Arf signaling.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsDiploidyGenes, FungalGenotypeGTP-Binding ProteinsHL-60 CellsHomozygoteHumansMeiosisPhospholipase DProto-Oncogene Proteins c-mycRecombinant Fusion ProteinsRecombinant ProteinsSaccharomyces cerevisiaeSpores, FungalADP-Ribosylation Factor 1ADP-Ribosylation FactorsARF4 protein, humanGTP-Binding ProteinsPhospholipase DProto-Oncogene Proteins c-mycRecombinant Fusion ProteinsRecombinant Proteins

Identifiers

PMID9693364
PMCPMC25455
OpenAlexW2096716792

What Socratic 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 Socratic graph.