Evidence map›Paper›PMID 14993293›Full record

ArticleMolecular and cellular biology2004

Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor.

Rina Plattner, Anthony J Koleske, Andrius Kazlauskas, Ann Marie Pendergast

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

45 citing papers in PubMed, 79 citations in OpenAlex.

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  19. Mesenchymal stem cells are sensitive to treatment with kinase inhibitors and ionizing radiation.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2014
    Article
  20. c-Abl activates janus kinase 2 in normal hematopoietic cells.The Journal of biological chemistry · 2014
    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

4 authors at 3 institutions in 1 country.

Rina PlattnerDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Anthony J Koleske
Andrius Kazlauskas
Ann Marie Pendergast
Duke Medical Center · USMassachusetts Eye and Ear Infirmary · USYale University · US

Funding

Viral Oncology Training GrantT32CA009111 · NCI · DUKE UNIVERSITY · PI LUFTIG, MICAH A. · 1985 to 2023
$8.9M
Roles of Abl and Arg Neuronal DevelopmentR01NS039475 · NINDS · YALE UNIVERSITY · PI KOLESKE, ANTHONY J · 2000 to 2012
$4.3M
MOLECULAR BASIS OF SIGNALING BY THE CABL PROTO-ONCOGENER01CA070940 · NCI · DUKE UNIVERSITY · PI PENDERGAST, ANN MARIE · 1996 to 2010
$3.4M
PDGF RECEPTOR-ASSOCIATED PROTEINS IN SIGNALINGR01GM048339 · NIGMS · SCHEPENS EYE RESEARCH INSTITUTE · PI KAZLAUSKAS, ANDRIUS · 1992 to 2003
$1.2M
TYROSINE KINASES AND ADAPTOR PROTEINS IN CELL MIGRATIONR01GM062375 · NIGMS · DUKE UNIVERSITY · PI PENDERGAST, ANN MARIE · 2001 to 2005
$784k
NCI NIH HHS CA09111-25NCI NIH HHS CA70940NCI NIH HHS R01 CA070940NCI NIH HHS T32 CA009111NIGMS NIH HHS GM48339NIGMS NIH HHS GM62375NIGMS NIH HHS R01 GM062375NINDS NIH HHS NS39475NINDS NIH HHS R01 NS039475
6 · The paper itself

Abstract

The c-Abl nonreceptor tyrosine kinase is activated by growth factor signals such as the platelet-derived growth factor (PDGF) and functions downstream of the PDGF-beta receptor (PDGFR) to mediate biological processes such as membrane ruffling, mitogenesis, and chemotaxis. Here, we show that the related kinase Arg is activated downstream of PDGFRs in a manner dependent on Src family kinases and phospholipase C gamma1 (PLC-gamma1)-mediated phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolysis, as we showed previously for c-Abl. PIP2, a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits the tyrosine kinase activities of both Arg and c-Abl in vitro and in cells. We now demonstrate that c-Abl and Arg form inducible complexes with and are phosphorylated by the PDGFR tyrosine kinase in vitro and in vivo. Moreover, c-Abl and Arg, in turn, phosphorylate the PDGFR. We show that c-Abl and Arg exhibit nonredundant functions downstream of the activated PDGFR. Reintroduction of c-Abl into Arg-Abl double-null fibroblasts rescues the ability of PLC-gamma1 to increase PDGF-mediated chemotaxis, while reexpression of Arg fails to rescue the chemotaxis defect. These data show that, although both kinases are activated and form complexes with proteins in the PDGFR signaling pathway, only c-Abl functions downstream of PLC-gamma1 to mediate chemotaxis.

Indexed as

AnimalsCell LineChemotaxisEnzyme ActivationIn Vitro TechniquesMacromolecular SubstancesMiceNIH 3T3 CellsPhospholipase C gammaPhosphorylationProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablReceptor, Platelet-Derived Growth Factor alphaReceptor, Platelet-Derived Growth Factor betaRecombinant ProteinsSignal TransductionARG tyrosine kinaseMacromolecular SubstancesPhospholipase C gammaProtein-Tyrosine KinasesProto-Oncogene Proteins c-ablReceptor, Platelet-Derived Growth Factor alphaReceptor, Platelet-Derived Growth Factor betaRecombinant ProteinsType C Phospholipases

Identifiers

PMID14993293
PMCPMC355852
OpenAlexW2128937539

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.