Evidence map›Paper›PMID 11046132›Full record

ArticleMolecular and cellular biology2000

Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activity.

S Maudsley, A M Zamah, N Rahman, J T Blitzer, L M Luttrell, R J Lefkowitz, R A Hall

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

84 citing papers in PubMed, 204 citations in OpenAlex.

  1. Review
  2. Article
  3. ERM-1 Phosphorylation and NRFL-1 Redundantly Control Lumen Formation in theFrontiers in cell and developmental biology · 2022
    Article
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  12. Review
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  16. Article
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  18. Article
  19. NHERF1 Enhances Cisplatin Sensitivity in Human Cervical Cancer Cells.International journal of molecular sciences · 2017
    Article
  20. Dynamic NHERF interaction with TRPC4/5 proteins is required for channel gating by diacylglycerol.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article

24 more citing papers are in PubMed but not listed here.

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 MaudsleyHoward Hughes Medical Institute, Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
A M Zamah
N Rahman
J T Blitzer
L M Luttrell
R J Lefkowitz
R A Hall
Howard Hughes Medical Institute · USDuke Medical Center · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
NHERF IN BETA-2-ADRENERGIC RECEPTOR SIGNALINGR01HL064713 · NHLBI · EMORY UNIVERSITY · PI HALL, RANDY A. · 2000 to 2003
$1.1M
MOLECULAR PROPERTIES OF CARDIAC ADRENERGIC RECEPTORSR37HL016037 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 1986 to 1995
–
NHLBI NIH HHS HL16037NHLBI NIH HHS HL64713NHLBI NIH HHS R01 HL016037NHLBI NIH HHS R01 HL064713
6 · The paper itself

Abstract

Platelet-derived growth factor (PDGF) is a potent mitogen for many cell types. The PDGF receptor (PDGFR) is a receptor tyrosine kinase that mediates the mitogenic effects of PDGF by binding to and/or phosphorylating a variety of intracellular signaling proteins upon PDGF-induced receptor dimerization. We show here that the Na(+)/H(+) exchanger regulatory factor (NHERF; also known as EBP50), a protein not previously known to interact with the PDGFR, binds to the PDGFR carboxyl terminus (PDGFR-CT) with high affinity via a PDZ (PSD-95/Dlg/Z0-1 homology) domain-mediated interaction and potentiates PDGFR autophosphorylation and extracellular signal-regulated kinase (ERK) activation in cells. A point-mutated version of the PDGFR, with the terminal leucine changed to alanine (L1106A), cannot bind NHERF in vitro and is markedly impaired relative to the wild-type receptor with regard to PDGF-induced autophosphorylation and activation of ERK in cells. NHERF potentiation of PDGFR signaling depends on the capacity of NHERF to oligomerize. NHERF oligomerizes in vitro when bound with PDGFR-CT, and a truncated version of the first NHERF PDZ domain that can bind PDGFR-CT but which does not oligomerize reduces PDGFR tyrosine kinase activity when transiently overexpressed in cells. PDGFR activity in cells can also be regulated in a NHERF-dependent fashion by stimulation of the beta(2)-adrenergic receptor, a known cellular binding partner for NHERF. These findings reveal that NHERF can directly bind to the PDGFR and potentiate PDGFR activity, thus elucidating both a novel mechanism by which PDGFR activity can be regulated and a new cellular role for the PDZ domain-containing adapter protein NHERF.

Indexed as

Amino Acid MotifsAnimalsCHO CellsCricetinaeGenes, DominantMitogen-Activated Protein KinasesPhosphoproteinsPhosphorylationPlatelet-Derived Growth FactorPoint MutationReceptors, Adrenergic, beta-2Receptors, Platelet-Derived Growth FactorRecombinant Fusion ProteinsSodium-Hydrogen ExchangersMitogen-Activated Protein KinasesPhosphoproteinsPlatelet-Derived Growth FactorReceptors, Adrenergic, beta-2Receptors, Platelet-Derived Growth FactorRecombinant Fusion Proteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen Exchangers

Identifiers

PMID11046132
PMCPMC102142
OpenAlexW2136205584

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.