Chronic Myeloid Leukemia (CML) is a clonal myeloproliferative disease characterized by the occurrence of the Bcr-Abl fusion oncoprotein, which resulted from a reciprocal translocation between chromosomes 9 and 22. The Golgi complex-localized protein 1(GLG1) was identified by mass spectrometry as a potential interaction partner to the pleckstrin homology (PH) domain of the Bcr-Abl oncoprotein. The GLG1 protein is a transmembrane protein known also as MG-160, ESL-1, and CFR-1. Irregularities in the GLG1 functions affect the adhesion, mobility, and migration of cells. In this study, the interaction between the GLG1 protein and the Bcr-Abl oncoprotein is shown for the first time. With imunofluorescence and confocal microscopy, colocalization of the GLG1protein and the Bcr-Abl oncoprotein to the Golgi complex has been detected. A GLG1 protein form phosphorylated at the tyrosine site in K562 cells has also been detected, and Tyr phosphorylation sites for GLG1 isoforms were predicted. The authors believe that the oncoprotein phosphorylates the GLG1 protein, at the cost of its Abl part, during the GLG1–Bcr-Abl protein interaction in the Golgi complex, thus affecting its activity and disrupting the descending signaling pathways that may be crucial for the development and progression of the disease.
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The authors declare that they have no conflict of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.
Translated by N. Tarasyuk
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Antonenko, S.V., Kravchuk, I.V. & Telegeev, G.D. Interaction of Bcl-Abl Oncoprotein with the Glg1 Protein in K562 Cells: its Role in the Pathogenesis of Chronic Myeloid Leukemia. Cytol. Genet. 54, 48–54 (2020). https://doi.org/10.3103/S0095452720010028
- chronic myeloid leukemia (CML)
- Bcr-Abl oncoprotein
- Golgi complex-localized glycoprotein 1(GLG1)
- Golgi complex
- K562 cells