Evidence map›Paper›PMID 16339153›Full record

ArticleThe Journal of biological chemistry2006

Kinetic analysis of a mammalian phospholipase D: allosteric modulation by monomeric GTPases, protein kinase C, and polyphosphoinositides.

Lee G Henage, John H Exton, H Alex Brown

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

32 citing papers in PubMed, 64 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Article
  5. Structure and regulation of human phospholipase D.Advances in biological regulation · 2021
    Review
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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

3 authors at 1 institution in 1 country.

Lee G HenageDepartment of Pharmacology, Institute for Chemical Biology, Vanderbilt University, Nashville, Tennessee 37232-6600, USA.
John H Exton
H Alex Brown
Vanderbilt University · US

Funding

PHOSPHOLIPASE ACTIVATION BY G-PROTEIN-LINKED RECEPTORSR01GM058516 · NIGMS · VANDERBILT UNIVERSITY · PI BROWN, ALEX · 2000 to 2004
$1.2M
NIGMS NIH HHS GM58516NIGMS NIH HHS R01 GM058516
6 · The paper itself

Abstract

In mammalian cells, phospholipase D activity is tightly regulated by diverse cellular signals, including hormones, neurotransmitters, and growth factors. Multiple signaling pathways converge upon phospholipase D to modulate cellular actions, such as cell growth, shape, and secretion. We examined the kinetics of protein kinase C and G-protein regulation of mammalian phospholipase D1 (PLD1) in order to better understand interactions between PLD1 and its regulators. Activation by Arf-1, RhoA, Rac1, Cdc42, protein kinase Calpha, and phosphatidylinositol 4,5-bisphosphate displayed surface dilution kinetics, but these effectors modulated different kinetic parameters. PKCalpha activation of PLD1 involves N- and C-terminal PLD domains. Rho GTPases were binding activators, enhancing the catalytic efficiency of a purified PLD1 catalytic domain via effects on Km. Arf-1, a catalytic activator, stimulated PLD1 by enhancing the catalytic constant, kcat. A kinetic description of PLD1 activation by multiple modulators reveals a mechanism for apparent synergy between activators. Synergy was observed only when PLD1 was simultaneously stimulated by a binding activator and a catalytic activator. Surprisingly, synergistic activation was steeply dependent on phosphatidylinositol 4,5-bisphosphate and phosphatidylcholine. Together, these findings suggest a role for PLD1 as a signaling node, in which integration of convergent signals occurs within discrete locales of the cellular membrane.

Indexed as

Adenosine DiphosphateADP-Ribosylation Factor 1Allosteric SiteAnimalsCatalysiscdc42 GTP-Binding ProteinCell MembraneChlorocebus aethiopsCOS CellsDose-Response Relationship, DrugEnzyme ActivationEscherichia coliGenetic VectorsGTP-Binding ProteinsKineticsModels, ChemicalAdenosine DiphosphateADP-Ribosylation Factor 1cdc42 GTP-Binding ProteinGTP-Binding ProteinsPhosphatidylcholinesPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhospholipase Dphospholipase D1Protein Kinase Crac1 GTP-Binding ProteinRecombinant ProteinsrhoA GTP-Binding ProteinSucrose

Identifiers

PMID16339153
PMCPMC3800466
OpenAlexW2005088092

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.