Abstract
Nemo-like kinase (NLK), a mediator of the Wnt signaling pathway, binds directly to c-Myb, leading to its phosphorylation, ubiquitination and proteasome-dependent degradation. NLK was significantly downregulated in the breast cancer tissues compared to corresponding normal tissues. NLK expression was negatively correlated with c-Myb expression. NLK suppressed proliferation, induced apoptosis and mediated c-Myb degradation in MCF-7 cells via a mechanism that seems to involve c-myc and Bcl2. These findings might provide a novel target for therapeutic intervention in patients with breast cancer.
MeSH terms
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Apoptosis*
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Breast Neoplasms / enzymology*
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Breast Neoplasms / genetics
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Breast Neoplasms / pathology*
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Cell Cycle
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Cell Proliferation
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Down-Regulation / genetics
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Female
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Humans
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Intracellular Signaling Peptides and Proteins / metabolism*
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Ki-67 Antigen / metabolism
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MCF-7 Cells
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Middle Aged
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Protein Serine-Threonine Kinases / metabolism*
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Proteolysis*
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Proto-Oncogene Proteins c-bcl-2 / metabolism
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Proto-Oncogene Proteins c-myb / metabolism*
Substances
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Intracellular Signaling Peptides and Proteins
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Ki-67 Antigen
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Proto-Oncogene Proteins c-bcl-2
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Proto-Oncogene Proteins c-myb
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NLK protein, human
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Protein Serine-Threonine Kinases
Grants and funding
The authors have no support or funding to report.