Cited by 19Chronic Myeloid Leukemia TreatmentsUbiquitin and proteasome pathwaysProtein Tyrosine Phosphatases

The DOI matches its Crossref record, with a small difference in title or year; 39 of the 39 references it cites were found in a registry or an index.

Inhibition of USP1, a new partner of Bcr-Abl, results in decrease of Bcr-Abl level in K562 cells

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Antonenko, S.V., Telegeev, G.D.·2023·Experimental Oncology

Abstract

AIM: 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. MATERIALS AND METHODS: The interaction between USP1 and Bcr-Abl in K562 cells was analyzed by co-immunoprecipitation, Western blot analysis, and confocal microscopy. RESULTS: 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. CONCLUSIONS: 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.

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Research works printed but not linked: 5

  1. [1]1. Salem А, Loghavi S, Tang G, et al . Myeloid neoplasms with concurrent BCR-ABL1 and CBFB rearrangements: A series of 10 cases of a clinically aggressive neoplasm. Am J Hematol 2017; 92 : 520-8.
  2. [6]6. Antonenko S, Gurianov D, Telegeev G. Colocalization of USP1 and РН domain of Bcr-Abl oncoprotein in terms of chronic myeloid leukemia cell rearrangements. Tsitol Genet 2016; 50 : 11-5.
  3. [20]20. Shibata N, Miyamoto N, Nagai K, et al . Development of protein degradation inducers of oncogenic BCR-ABL pro- - tein by conjugation of ABL kinase inhibitors and IAP ligands. Cancer Sci 2017; 108 : 1657-66.
  4. [38]38. Gorrepati K, Lupse B, Annamalai K, et al. Loss of deubiquitinase USP1 blocks pancreatic β-cell apoptosis by inhibiting DNA damage response. iScience 2018; 23: 72-86.
  5. [41]41. Goldbraikh D, Neufeld D, Eid-Mutlak Y, et al. USP1 deubiquitinates protein kinase Akt to inhibit PI3K-AktFoxO signaling in muscle during prolonged starvation. EMBO Rep 2020; 21 : e48791.

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Metadata

Authors
Antonenko, S. V., & Telegeev, G. D.
Affiliations
Institute of Molecular Biology and Genetics (UA)
Venue
Experimental Oncology
Published
2023-06-01
Volume
42
Issue
2
Pages
109-114
ISSN
  • 0204-3564 (ISSN-L)
  • 2312-8852
  • 1812-9269
OpenAlex
W3038319487
Cited by
19
References
39
Citations by year
2026: 5 · 2025: 2 · 2024: 4 · 2023: 4
FWCI
1.26
Type
journal article
Language
en
Open access
Locations
  • Experimental Oncology (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Chronic Myeloid Leukemia Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
USP1, BCR-ABL, chronic myeloid leukemia, K562 cells, protein-protein interaction, nuclear protein complex, targeted therapy
MeSH terms
Cell Nucleus, Humans, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Fusion Proteins, bcr-abl, K562 Cells, Ubiquitin-Specific Proteases

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CoChat. (2026). Citation check: Inhibition of USP1, a new partner of Bcr-Abl, results in decrease of Bcr-Abl level in K562 cells. https://app.cochat.ai/papers/10.32471/exp-oncology.2312-8852.vol-42-no-2.14533
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Antonenko, S. V., & Telegeev, G. D. (2023). Inhibition of USP1, a new partner of Bcr-Abl, results in decrease of Bcr-Abl level in K562 cells. Experimental Oncology. https://doi.org/10.32471/exp-oncology.2312-8852.vol-42-no-2.14533