Evidence map›Paper›PMID 17000758›Full record

ArticleMolecular and cellular biology2006

Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs.

Elena V Kostenko, Oyenike O Olabisi, Sutapa Sahay, Pedro L Rodriguez, Ian P Whitehead

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  7. ER-phagy and human diseases.Cell death and differentiation · 2020
    Review
  8. Emerging Principles of Selective ER Autophagy.Journal of molecular biology · 2020
    Review
  9. Review
  10. Article
  11. Article
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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

5 authors at 2 institutions in 1 country.

Elena V KostenkoDepartment of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, Newark, NJ 07101-1709, USA.
Oyenike O Olabisi
Sutapa Sahay
Pedro L Rodriguez
Ian P Whitehead
University Hospital, Newark · USRutgers New Jersey Medical School

Funding

Novel Pathways for Bcr-Abl transformationR01CA097066 · NCI · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI WHITEHEAD, IAN P · 2003 to 2012
$2.5M
Sec14 Domain-Mediated Regulation of the Dbs OncogeneF32CA113049 · NCI · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI KOSTENKO, ELENA V · 2005 to 2006
$76k
Minority Predoctoral Fellowship ProgramF31CA117049 · NCI · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI OLABISI, OYENIKE · 2005 to 2008
$66k
NCI NIH HHS CA 113049NCI NIH HHS CA 117049NCI NIH HHS CA 97066NCI NIH HHS F31 CA117049NCI NIH HHS F32 CA113049NCI NIH HHS R01 CA097066
6 · The paper itself

Abstract

Dbs is a Rho-specific guanine nucleotide exchange factor (RhoGEF) with in vitro exchange activity specific for RhoA and Cdc42. Like many RhoGEF family members, the in vivo exchange activity of Dbs is restricted in a cell-specific manner. Here we report the characterization of a novel scaffold protein (designated cell cycle progression protein 1 [Ccpg1]) that interacts with Dbs and modulates its in vivo exchange specificity. When coexpressed in mammalian cells, Ccpg1 binds to the Dbl homology/pleckstrin homology domain tandem motif of Dbs and inhibits its exchange activity toward RhoA, but not Cdc42. Expression of Ccpg1 correlates with the ability of Dbs to activate endogenous RhoA in cultured cells, and suppression of endogenous Ccpg1 expression potentiates Dbs exchange activity toward RhoA. The isolated Dbs binding domain of Ccpg1 is not sufficient to suppress Dbs exchange activity on RhoA, thus suggesting a regulatory interaction. Ccpg1 mediates recruitment of endogenous Src kinase into Dbs-containing complexes and interacts with the Rho family member Cdc42. Collectively, our studies suggest that Ccpg1 represents a new class of regulatory scaffold protein that can function as both an assembly platform for Rho protein signaling complexes and a regulatory protein which can restrict the substrate utilization of a promiscuous RhoGEF family member.

Indexed as

Amino Acid SequenceAnimalsBinding Sitescdc42 GTP-Binding ProteinCell Cycle ProteinsCell LineCell Transformation, NeoplasticChlorocebus aethiopsCOS CellsEnzyme ActivationEscherichia coliFibroblastsGenes, ReporterGlutathione TransferaseGuanine Nucleotide Exchange FactorsHemagglutininsCcpg1 protein, mousecdc42 GTP-Binding ProteinCell Cycle ProteinsGlutathione TransferaseGuanine Nucleotide Exchange FactorsHemagglutininsLuciferasesMcf2l protein, mouseProteinsRecombinant Fusion ProteinsrhoA GTP-Binding ProteinRho Guanine Nucleotide Exchange Factors

Identifiers

PMID17000758
PMCPMC1636807
OpenAlexW2144460410

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.