Institute of Molecular Biology and Genetics NAS of Ukraine, Kyiv 03143, Ukraine.
Exp Oncol. 2020 Jun;42(2):109-114. doi: 10.32471/exp-oncology.2312-8852.vol-42-no-2.14533.
To analyze interaction of ubiquitin specific peptidase 1 (USP1) with Bcr-Abl and to assess the relation between USP1 functional activity and Bcr-Abl expression in K562 chronic myeloid leukemia cells.
The interaction between USP1 and Bcr-Abl in K562 cells was analyzed by co-immunoprecipitation, Western blot analysis, and confocal microscopy.
A direct interaction between Bcr-Abl oncoprotein and USP1 protein in K562 cells was established by co-immunoprecipitation. Immunofluorescence analysis and confocal microscopy revealed that Bcr-Abl/USP1 protein complex is formed in the cell nucleus. The inhibition of USP1 protein activity by ML323 reduced the level of Bcr-Abl oncoprotein in K562 cells.
USP1 protein has been identified as a new protein partner of Bcr-Abl oncoprotein in chronic myeloid leukemia. The relationship between the functional activity of USP1 protein and the level of Bcr-Abl oncoprotein has been demonstrated, suggesting that the targeted inhibition of USP1 activity could be a challenging approach for reducing Bcr-Abl expression.
分析泛素特异性肽酶 1（USP1）与 Bcr-Abl 的相互作用，并评估 K562 慢性髓系白血病细胞中 USP1 功能活性与 Bcr-Abl 表达之间的关系。
通过共免疫沉淀、Western blot 分析和共聚焦显微镜分析来分析 USP1 与 Bcr-Abl 在 K562 细胞中的相互作用。
通过共免疫沉淀证实了 Bcr-Abl 癌蛋白与 K562 细胞中 USP1 蛋白之间的直接相互作用。免疫荧光分析和共聚焦显微镜显示，Bcr-Abl/USP1 蛋白复合物在细胞核中形成。USP1 蛋白活性的抑制通过 ML323 降低了 K562 细胞中 Bcr-Abl 癌蛋白的水平。
USP1 蛋白已被鉴定为慢性髓系白血病中 Bcr-Abl 癌蛋白的新蛋白伴侣。证明了 USP1 蛋白的功能活性与 Bcr-Abl 癌蛋白水平之间的关系，提示靶向抑制 USP1 活性可能是降低 Bcr-Abl 表达的一种有挑战性的方法。
