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Targeting mitophagy in SRSF2 mutant hematologic malignancies

Liu, X.; Devadiga, S. A.; Stanley, R. F.; Moroow, R.; Janssen, K.; Quesnel-Vallieres, M.; Pomp, O.; Moverley, A. A.; Li, C.; Skuli, N.; Carroll, M. P.; Huang, J.; Wallace, D. C.; Lynch, K. W.; Abdel-Wahab, O.; Klein, P. S.

2023-06-25 cancer biology
10.1101/2023.06.25.546449 bioRxiv
Show abstract

Splicing factor mutations are common in myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML), but how they alter cellular functions is unclear. We show that the pathogenic SRSF2P95H/+ mutation disrupts the splicing of mitochondrial mRNAs, impairs mitochondrial complex I function, and robustly increases mitophagy. We also identified a mitochondrial surveillance mechanism by which mitochondrial dysfunction modifies splicing of the mitophagy activator PINK1 to remove a poison intron, increasing the stability and abundance of PINK1 mRNA and protein. SRSF2P95H-induced mitochondrial dysfunction increased PINK1 expression through this mechanism, which is essential for survival of SRSF2P95H/+ cells. Inhibition of splicing with a glycogen synthase kinase 3 inhibitor promoted retention of the poison intron, impairing mitophagy and activating apoptosis in SRSF2P95H/+ cells. These data reveal a homeostatic mechanism for sensing mitochondrial stress through PINK1 splicing and identify increased mitophagy as a disease marker and a therapeutic vulnerability in SRSF2P95H mutant MDS and AML.

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