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Here, we identify the lipid kinase PIKfyve as overexpressed in NEPC, functioning as a central node in a stress-lipid kinase axis that drives adaptation to persistent endoplasmic reticulum (ER) stress. Mechanistically, NEPC requires PIKfyve-mediated lysosomal degradation and lipid recycling to maintain metabolic homeostasis under hypoxia. PIKfyve inhibition disrupts lysosomal function, leading to ER stress accumulation and activation of a compensatory, sterol regulatory element-binding protein (SREBP)-dependent de novo lipogenesis program essential for NEPC survival. This stress-lipid axis creates a synthetic vulnerability between PIKfyve and fatty acid synthase (FASN), where dual inhibition synergistically amplifies ER stress, triggers the terminal unfolded protein response, and induces tumor cell death. These findings reveal a metabolic adaptation in NEPC and provide preclinical evidence that co-targeting PIKfyve and FASN can overcome hypoxia-associated stress adaptation.<\/jats:p>","DOI":"10.64898\/2026.06.15.732391","type":"posted-content","created":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T22:00:14Z","timestamp":1781820014000},"source":"Crossref","is-referenced-by-count":0,"title":["A Stress-Adaptive Lipid Kinase Axis Defines Metabolic Vulnerabilities in Neuroendocrine Prostate Cancer"],"prefix":"10.64898","author":[{"given":"Yang","family":"Zheng","sequence":"first","affiliation":[{"name":"Michigan Center for Translational Pathology, University of Michigan, Ann Arbor, MI, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Caleb","family":"Cheng","sequence":"additional","affiliation":[{"name":"Michigan Center for Translational Pathology, University of Michigan, Ann Arbor, MI, 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