Abstract 1652 Structural and Functional Characterization on the SCP4-STK35 Phospho-Signaling Complex

Acute myeloid leukemia (AML) is a devastating blood cancer driven by aberrant signaling pathways that promote uncontrolled cell proliferation. Small C-terminal phosphatase 4 (SCP4), encoded by CTDSPL2, has been identified as a phosphatase critical for AML survival while being dispensable in normal blood cells, highlighting its potential as a selective therapeutic target. SCP4 interacts with two paralogous kinases, STK35 and PDIK1L, which act as both substrates and interacting partners to drive AML proliferation.