학술논문

Hyperphosphorylation of BCL-2 family proteins underlies functional resistance to venetoclax in lymphoid malignancies.
Document Type
article
Source
Journal of Clinical Investigation. 133(22)
Subject
Apoptosis survival pathways
Hematology
Oncology
Phosphoprotein phosphatases
Protein kinases
Mice
Animals
Humans
Leukemia
Lymphocytic
Chronic
B-Cell
Drug Resistance
Neoplasm
Proto-Oncogene Proteins c-bcl-2
Bridged Bicyclo Compounds
Heterocyclic
bcl-X Protein
Apoptosis Regulatory Proteins
Lymphoma
Large B-Cell
Diffuse
Cell Line
Tumor
Antineoplastic Agents
Apoptosis
Myeloid Cell Leukemia Sequence 1 Protein
Language
Abstract
The B cell leukemia/lymphoma 2 (BCL-2) inhibitor venetoclax is effective in chronic lymphocytic leukemia (CLL); however, resistance may develop over time. Other lymphoid malignancies such as diffuse large B cell lymphoma (DLBCL) are frequently intrinsically resistant to venetoclax. Although genomic resistance mechanisms such as BCL2 mutations have been described, this probably only explains a subset of resistant cases. Using 2 complementary functional precision medicine techniques - BH3 profiling and high-throughput kinase activity mapping - we found that hyperphosphorylation of BCL-2 family proteins, including antiapoptotic myeloid leukemia 1 (MCL-1) and BCL-2 and proapoptotic BCL-2 agonist of cell death (BAD) and BCL-2 associated X, apoptosis regulator (BAX), underlies functional mechanisms of both intrinsic and acquired resistance to venetoclax in CLL and DLBCL. Additionally, we provide evidence that antiapoptotic BCL-2 family protein phosphorylation altered the apoptotic protein interactome, thereby changing the profile of functional dependence on these prosurvival proteins. Targeting BCL-2 family protein phosphorylation with phosphatase-activating drugs rewired these dependencies, thus restoring sensitivity to venetoclax in a panel of venetoclax-resistant lymphoid cell lines, a resistant mouse model, and in paired patient samples before venetoclax treatment and at the time of progression.