Evidence map›Paper›PMID 20628057›Full record

ArticleThe Journal of biological chemistry2010

Post-transcriptional mechanisms contribute to the suppression of the ErbB3 negative regulator protein Nrdp1 in mammary tumors.

Ellen Q Ingalla, Jamie K Miller, Jessica H Wald, Heather C Workman, Rouminder P Kaur, Lily Yen, William H D Fry, Alexander D Borowsky, Lawrence J T Young, Colleen Sweeney and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

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  16. E3 ubiquitin ligases in ErbB receptor quantity control.Seminars in cell & developmental biology · 2010
    Review
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

11 authors at 1 institution in 1 country.

Ellen Q IngallaUniversity of California Davis Cancer Center, Sacramento, California 95817, USA.
Jamie K Miller
Jessica H Wald
Heather C Workman
Rouminder P Kaur
Lily Yen
William H D Fry
Alexander D Borowsky
Lawrence J T Young
Colleen Sweeney
Kermit L Carraway
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
LABORATORY MEDICINE TRAINING PROGRAMT32RR007038 · NCRR · UNIVERSITY OF CALIFORNIA DAVIS · PI BARTHOLD, STEPHEN WILLIAM · 1988 to 2011
$4.0M
NRDP1 PROTEIN DEGRADATION PATHWAY IN MAMMARY TUMOR PROGRESSIONR01CA123541 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CARRAWAY, KERMIT L · 2006 to 2016
$2.5M
Mechanisms of Receptor Tyrosine Kinase InhibitionR01CA118384 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SWEENEY, COLLEEN ANN · 2006 to 2016
$2.4M
Modulation of ErbB Receptor Tyrosine Kinase SignalingR01GM068994 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CARRAWAY, KERMIT L · 2003 to 2011
$2.4M
UCD Mouse Biology Program: Pathology Resources Training and Cancer ModelingK26RR024037 · NCRR · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BOROWSKY, ALEXANDER D · 2007 to 2011
$717k
NCI NIH HHS CA118384NCI NIH HHS CA123541NCI NIH HHS P30 CA093373NCI NIH HHS R01 CA118384NCI NIH HHS R01 CA123541NCRR NIH HHS K26 RR024037NCRR NIH HHS T32 RR007038NCRR NIH HHS T32 RR07038NIGMS NIH HHS GM068994NIGMS NIH HHS R01 GM068994
6 · The paper itself

Abstract

The ErbB2 and ErbB3 receptor tyrosine kinases act synergistically to promote cellular properties associated with tumor development. Previous studies indicate that endogenous ErbB3 protein is markedly elevated in mouse mammary tumors induced by transgenic ErbB2 overexpression. However, this occurs in the absence of elevated ErbB3 transcript, indicating that post-transcriptional regulatory mechanisms play crucial roles in suppressing ErbB3 protein in normal tissue. Our previous studies also demonstrate that protein levels of Nrdp1, an E3 ubiquitin ligase that targets ErbB3 for degradation, are markedly suppressed in tumors from ErbB2 transgenic animals relative to normal tissue. Here we demonstrate that transgenic expression of Nrdp1 cDNA in the mouse mammary gland is not sufficient to suppress elevated ErbB3 levels or tumor initiation and growth in ErbB2 transgenic mice. Unexpectedly, Nrdp1 protein is absent in tumors from Nrdp1/ErbB2 bigenic mice, and real time PCR analysis indicates that Nrdp1 protein levels are suppressed post-transcriptionally. Nrdp1 protein is more resistant to proteasome-dependent degradation when exogenously expressed in cultured MCF10A nontransformed human breast epithelial cells than in breast tumor cells. These observations indicate that mammary tumors use potent post-transcriptional mechanisms to suppress Nrdp1 protein levels and that protein destabilization may play a central role in Nrdp1 loss in tumors.

Indexed as

AnimalsBreast NeoplasmsCarrier ProteinsCell LineErb-b2 Receptor Tyrosine KinasesFemaleHumansMammary Glands, AnimalMammary Neoplasms, AnimalMiceMice, TransgenicProtein StabilityReceptor, ErbB-3Ubiquitin-Protein LigasesCarrier ProteinsERBB2 protein, humanErbb2 protein, mouseErb-b2 Receptor Tyrosine KinasesReceptor, ErbB-3RNF41 protein, humanRnf41 protein, mouseUbiquitin-Protein Ligases

Identifiers

PMID20628057
PMCPMC2937896
OpenAlexW2083559436

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.