Jukka K. Westermarck

This study shows that disrupting the CIP2A gene reduces T cell-driven inflammation in experimental autoimmune encephalomyelitis.

This study identifies a druggable pocket on CIP2A that modulates its dimerization, PP2A interaction, and stability, with GNA as a tool compound that disrupts these functions.

This study shows that activating PP2A-B56 in PDAC increases EGFR signaling and promotes tumor growth, suggesting a new therapeutic target.

This study identifies enhanced mitochondrial respiration and glutamine-dependent TCA cycle as vulnerabilities in MYChigh breast cancer cells, showing synthetic lethality with complex I inhibitors.

This paper identifies S166 phosphorylation on LSD1 as a regulatory switch that controls gene activation, chromatin remodeling, and tumor microenvironment in non-hormonal cancer cells.

The paper identifies a PP2A-Integrator complex that opposes CDK9 activity to regulate transcription and shows its therapeutic synergy in leukemia.

The paper characterizes the CIP2A interactome in Th17 cells using affinity-purification mass spectrometry and validates key interactions, revealing associations with RNA processing and other cellular processes.

This study identifies UBR5 as a novel MYC ubiquitin ligase that regulates MYC protein stability and apoptotic threshold in cancer cells and breast tissue.

The paper presents a systemic analysis of PP2A-regulated phosphosignaling and drug responses, revealing rules for phosphoregulation and cancer therapy classification.