Differential signaling networks of Bcr–Abl p210 and p190 kinases in leukemia cells defined by functional proteomics View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-07

AUTHORS

S Reckel, R Hamelin, S Georgeon, F Armand, Q Jolliet, D Chiappe, M Moniatte, O Hantschel

ABSTRACT

The two major isoforms of the oncogenic Bcr-Abl tyrosine kinase, p210 and p190, are expressed upon the Philadelphia chromosome translocation. p210 is the hallmark of chronic myelogenous leukemia, whereas p190 occurs in the majority of B-cell acute lymphoblastic leukemia. Differences in protein interactions and activated signaling pathways that may be associated with the different diseases driven by p210 and p190 are unknown. We have performed a quantitative comparative proteomics study of p210 and p190. Strong differences in the interactome and tyrosine phosphoproteome were found and validated. Whereas the AP2 adaptor complex that regulates clathrin-mediated endocytosis interacts preferentially with p190, the phosphatase Sts1 is enriched with p210. Stronger activation of the Stat5 transcription factor and the Erk1/2 kinases is observed with p210, whereas Lyn kinase is activated by p190. Our findings provide a more coherent understanding of Bcr-Abl signaling, mechanisms of leukemic transformation, resulting disease pathobiology and responses to kinase inhibitors. More... »

PAGES

1502

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/leu.2017.36

DOI

http://dx.doi.org/10.1038/leu.2017.36

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1074195029

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28111465


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