Evidence map›Paper›PMID 9520417›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Functional association between Arf and RalA in active phospholipase D complex.

J Q Luo, X Liu, P Frankel, T Rotunda, M Ramos, J Flom, H Jiang, L A Feig, A J Morris, R A Kahn and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 132 citations in OpenAlex.

  1. Review
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  16. Article
  17. Honokiol suppresses survival signals mediated by Ras-dependent phospholipase D activity in human cancer cells.Clinical cancer research : an official journal of the American Association for Cancer Research · 2008
    Article
  18. Phospholipase D1 is an effector of Rheb in the mTOR pathway.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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

11 authors at 5 institutions in 2 countries.

J Q LuoDepartment of Biological Sciences, Hunter College of The City University of New York, New York, NY 10021, USA.
X Liu
P Frankel
T Rotunda
M Ramos
J Flom
H Jiang
L A Feig
A J Morris
R A Kahn
D A Foster
Tufts University · USHunter College · USCity University of New York · USEmory University · USState University of New York · US

Funding

WILD TYPE &MUTANT P53 INTERACTIONS WITH HIV LTR DNAG12RR003037 · NCRR · HUNTER COLLEGE · PI DOTTIN, ROBERT P · 1985 to 2011
$27.6M
Role of phospholipase D in tumorigenesisR01CA046677 · NCI · HUNTER COLLEGE · PI FOSTER, DAVID A · 1997 to 2014
$3.6M
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
BASIS FOR TRANSFORMATION BY FUJINAMI SARCOMA VIRUSR29CA046677 · NCI · HUNTER COLLEGE · PI FOSTER, DAVID A · 1989 to 1993
–
NCI NIH HHS CA46677NCI NIH HHS R01 CA046677NCRR NIH HHS G12 RR003037NCRR NIH HHS RR 03037NIGMS NIH HHS GM47707NIGMS NIH HHS R01 GM050388
6 · The paper itself

Abstract

Activation of phospholipase D1 (PLD1) by Arf has been implicated in vesicle transport and membrane trafficking. PLD1 has also been shown to be associated with the small GTPase RalA, which functions downstream from Ras in a Ras-RalA GTPase cascade that facilitates intracellular signal transduction. Although PLD1 associates directly with RalA, RalA has no effect upon the activity of PLD1. However, PLD1 precipitated from cell lysates with immobilized glutathione S-transferase-RalA fusion protein is active. This suggests the presence of an additional activating factor in the active RalA-PLD1 complexes. Because Arf stimulates PLD1, we looked for the presence of Arf in the active RalA-PLD1 complexes isolated from v-Src- and v-Ras-transformed cell lysates. Low levels of Arf protein were detected in RalA-PLD1 complexes; however, if guanosine 5'-[gamma-thio]triphosphate was added to activate Arf and stimulate translocation to the membrane, high levels of Arf were precipitated by RalA from cell lysates. Interestingly, deletion of 11 amino-terminal amino acids unique to Ral GTPases, which abolished the ability of RalA to precipitate PLD activity, prevented the association between RalA and Arf. Brefeldin A, which inhibits Arf GDP-GTP exchange, inhibited PLD activity in v-Src- and v-Ras-transformed cells but not in the nontransformed cells, suggesting that the association of Arf with RalA is required for the increased PLD activity induced by v-Src and v-Ras. These data implicate Arf in the transduction of intracellular signals activated by v-Src and mediated by the Ras-RalA GTPase cascade. Because both Arf and PLD1 stimulate vesicle formation in the Golgi, these data raise the possibility that vesicle formation and trafficking may play a role in the transduction of intracellular signals.

Indexed as

3T3 CellsADP-Ribosylation FactorsAnimalsEnzyme ActivationGTP-Binding ProteinsMiceMice, Inbred BALB CPhospholipase Dral GTP-Binding ProteinsSignal TransductionADP-Ribosylation FactorsGTP-Binding ProteinsPhospholipase Dral GTP-Binding Proteins

Identifiers

PMID9520417
PMCPMC19887
OpenAlexW1973834617

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.