Evidence map›Paper›PMID 11857085›Full record

ArticleOncogene2002

Differential expression and signaling of CBL and CBL-B in BCR/ABL transformed cells.

Martin Sattler, Yuri B Pride, Laura R Quinnan, Shalini Verma, Nicole A Malouf, Hervé Husson, Ravi Salgia, Stanley Lipkowitz, James D Griffin

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. 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
1.3field-weighted citation impact, top 21% 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, 29 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Martin SattlerDepartment of Adult Oncology, Dana-Farber Cancer Institute, 44 Binney Street, Boston, Massachusetts 02115, USA. martin_sattler@dfci.harvard.edu
Yuri B Pride
Laura R Quinnan
Shalini Verma
Nicole A Malouf
Hervé Husson
Ravi Salgia
Stanley Lipkowitz
James D Griffin
Dana-Farber Cancer Institute · USDana-Farber/Harvard Cancer Center · USNaval Medical Research Command · US

Funding

SIGNAL TRANSDUCTION PATHWAYS IN STABLE PHASE CHRONIC MYELOID LEUKEMIA CELLSP01DK050654 · NIDDK · DANA-FARBER CANCER INSTITUTE · PI D'ANDREA, ALAN DAVID · 1996 to 2006
$10.3M
NCI NIH HHS CA78348NIDDK NIH HHS DK50654
6 · The paper itself

Abstract

CBL and the related CBL-B protein are two members of a family of RING finger type ubiquitin E3 ligases that are believed to function as negative regulators of signal transduction in hematopoietic and immune cells. In mice, expression of v-Cbl causes lymphomas, and targeted disruption of either the CBL gene or the CBL-B gene can result in a lymphoproliferative disorder or hypersensitivity of lymphocytes. CBL is one of the most prominent targets of the BCR/ABL tyrosine kinase oncogene. We compared the role of CBL and CBL-B in signal transduction of BCR/ABL using pairs of cell lines before and after expression of BCR/ABL. In contrast to CBL, BCR/ABL was found to rapidly downregulate the expression of CBL-B protein. The decrease in CBL-B protein induced by BCR/ABL was associated with downregulation of CBL-B mRNA. Downregulation and tyrosine phosphorylation of CBL-B required BCR/ABL kinase activity. However, despite their known similarities in structure and function, we found CBL and CBL-B proteins to be involved in distinct signaling complexes. CBL was predominantly in a complex with phosphatidylinositol 3'-kinase and CRKL, while CBL-B was not associated with any significant phosphatidylinositol 3'-kinase activity. A major CBL-B associated protein was identified as mono-ubiquitinated Vav, a nucleotide exchange factor for Rac1. These results demonstrate that BCR/ABL signals differentially through CBL and CBL-B, with downregulation of the CBL-B protein potentially contributing to BCR/ABL-mediated transformation.

Indexed as

Adaptor Proteins, Signal TransducingSignal TransductionUbiquitin-Protein LigasesAnimalsCarrier ProteinsCell Line, TransformedCell MovementCell Transformation, NeoplasticDown-RegulationFusion Proteins, bcr-ablGene Expression Regulation, NeoplasticGenes, ablHumansHydrogen PeroxideMiceNuclear ProteinsAdaptor Proteins, Signal TransducingCarrier ProteinsCBLB protein, humanCblb protein, mouseCRKL proteinFusion Proteins, bcr-ablHydrogen PeroxideNuclear ProteinsOncogene ProteinsOncogene Protein v-cblPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotyrosinePIM1 protein, humanPim1 protein, mouseProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-cblProto-Oncogene Proteins c-pim-1Proto-Oncogene Proteins c-vavRetroviridae Proteins, OncogenicRNA, MessengerUbiquitin-Protein LigasesVAV1 protein, humanVav1 protein, mouse

Identifiers

PMID11857085
OpenAlexW1991987829

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.