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Bcr-Abl oncoprotein interacts with GLG1 in K562 cells: role in pathogenesis of chronic myeloid leukemia
SUMMARY. Chronic Myeloid Leukemia (CML) is a clonal myeloproliferative disease characterized by the appearance of a hybrid Bcr-Abl oncoprotein as a result of reciprocal translocation between chromosomes 9 and 22. GLG1 protein was identified as a potential partner for interaction with the PH domain of the Bcr-Abl oncoprotein by mass spectrometric analysis. GLG1 protein is a transmembrane protein, also known as MG-160, ESL-1, CFR-1. Disruption in the functioning of the GLG1 protein affects adhesion, mobility, and migration of cells. In our work, we first demonstrated the interaction of the GLG1 protein and Bcr-Abl oncoprotein. Using immunofluorescent analysis and confocal microscopy, we detected colocalization of GLG1 protein and Bcr-Abl oncoprotein in the Golgi complex. We also detected thyrosine phosphorylated form of the GLG1 protein in K562 cells and predicted Tyr phosphorylation sites for isoforms of GLG1 protein. We believe that during the interaction of GLG1 and Bcr-Abl proteins in the Golgi complex, oncoprotein phosphorylates the GLG1 protein due to its Abl part, thus affecting its activity and disrupting the downstream signaling pathways that may be critical for the development and progression of the disease.
Key words: Chronic Myeloid Leukemia (CML), Bcr-Abl oncoprotein, Golgi Glycoprotein 1 (GLG1), Golgi complex, Ê562 cell
E-mail: antonenkoimbg gmail.com
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