Evidence map›Paper›PMID 9447972›Full record

ArticleMolecular and cellular biology1998

Characterization of a Rac1- and RhoGDI-associated lipid kinase signaling complex.

K F Tolias, A D Couvillon, L C Cantley, C L Carpenter

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 144 citations in OpenAlex.

  1. A RAC1 SUMOylation switch governs breast cancer metastasis.Signal transduction and targeted therapy · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    Review
  6. DGK-θ: Structure, Enzymology, and Physiological Roles.Frontiers in cell and developmental biology · 2016
    Review
  7. Article
  8. Article
  9. Review
  10. Article
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  12. Article
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  17. 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

4 authors at 2 institutions in 3 countries.

K F ToliasBeth Israel Deaconess Medical Center, and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA. ktolias@bidmc.harvard.edu
A D Couvillon
L C Cantley
C L Carpenter
Hadassah Medical Center · ILInstitute of Cell Biology · UA

Funding

The Role of PI3K in Growth RegulationR01GM041890 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI CANTLEY, LEWIS C. · 1990 to 2016
$4.1M
PHOSPHATIDYLINOSITOL KINASESR01GM036624 · NIGMS · TUFTS UNIVERSITY BOSTON · PI CANTLEY, LEWIS C. · 1986 to 2008
$2.9M
Regulation of actin by Rac and PhosphoinositidesR01GM054389 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI CARPENTER, CHRISTOPHER · 1996 to 2005
$1.4M
NIGMS NIH HHS GM36624NIGMS NIH HHS GM54389NIGMS NIH HHS R01 GM036624NIGMS NIH HHS R01 GM041890NIGMS NIH HHS R01 GM054389
6 · The paper itself

Abstract

Rho family GTPases regulate a number of cellular processes, including actin cytoskeletal organization, cellular proliferation, and NADPH oxidase activation. The mechanisms by which these G proteins mediate their effects are unclear, although a number of downstream targets have been identified. The interaction of most of these target proteins with Rho GTPases is GTP dependent and requires the effector domain. The activation of the NADPH oxidase also depends on the C terminus of Rac, but no effector molecules that bind to this region have yet been identified. We previously showed that Rac interacts with a type I phosphatidylinositol-4-phosphate (PtdInsP) 5-kinase, independent of GTP. Here we report the identification of a diacylglycerol kinase (DGK) which also associates with both GTP- and GDP-bound Rac1. In vitro binding analysis using chimeric proteins, peptides, and a truncation mutant demonstrated that the C terminus of Rac is necessary and sufficient for binding to both lipid kinases. The Rac-associated PtdInsP 5-kinase and DGK copurify by liquid chromatography, suggesting that they bind as a complex to Rac. RhoGDI also associates with this lipid kinase complex both in vivo and in vitro, primarily via its interaction with Rac. The interaction between Rac and the lipid kinases was enhanced by specific phospholipids, indicating a possible mechanism of regulation in vivo. Given that the products of the PtdInsP 5-kinase and the DGK have been implicated in several Rac-regulated processes, and they bind to the Rac C terminus, these lipid kinases may play important roles in Rac activation of the NADPH oxidase, actin polymerization, and other signaling pathways.

Indexed as

Guanine Nucleotide Dissociation InhibitorsSignal TransductionAmino Acid SequenceAnimalsCell DivisionCOS CellsDiacylglycerol KinaseEnzyme ActivationGTP-Binding ProteinsMacromolecular SubstancesMolecular Sequence DataNADPH OxidasesPhospholipidsPhosphotransferases (Alcohol Group Acceptor)Protein BindingRats1-phosphatidylinositol-4-phosphate 5-kinaseDiacylglycerol KinaseGTP-Binding ProteinsGuanine Nucleotide Dissociation InhibitorsMacromolecular SubstancesNADPH OxidasesPhospholipidsPhosphotransferases (Alcohol Group Acceptor)rho-Specific Guanine Nucleotide Dissociation Inhibitors

Identifiers

PMID9447972
PMCPMC108787
OpenAlexW2142055861

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.