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Lactate is increasingly recognized not merely as a metabolic byproduct, but as a signaling metabolite capable of reshaping iron homeostasis and ferroptosis-related programs. Recent evidence has established that lactate induces hepatic hepcidin through soluble adenylyl cyclase (sAC)-dependent cAMP signaling, while separate lines of investigation have shown that lactate-associated protein lactylation can promote ferroptosis in selected pathological settings. Yet the upstream mechanism linking these two lactate-responsive modules remains unresolved. Here, we propose a focused mechanistic framework in which lactate-induced sAC/cAMP signaling contributes to the priming of lactyltransferases, particularly KAT8, thereby coupling rapid metabolic sensing to delayed, selective lactylation-dependent ferroptotic remodeling. This hypothesis is sharpened by recent evidence that lactate-primed KAT8 lactylates PCK2 at Lys100 and exacerbates ferroptosis during hepatic ischemia-reperfusion injury, although the basis of this priming event remains unknown. We integrate the currently available evidence supporting the lactate-sAC-hepcidin and lactate-KAT8-PCK2-ferroptosis axes, identify KAT8 priming as the key unresolved mechanistic step, and discuss plausible upstream routes including PKA-dependent regulation, lactyl-CoA supply through ACSS2, and alternative lactate-sensing pathways. We further outline experimentally testable predictions that could discriminate between signaling-dependent priming, donor-availability models, and substrate-accessibility mechanisms. Rather than advancing a disease-generalized pathway, this Perspective defines a narrower and testable upstream hypothesis that may clarify how metabolic stress, iron regulation, and selective protein lactylation converge in ferroptosis-prone states. The proposed sAC-KAT8 connection should therefore be viewed as a biologically plausible but still unproven mechanism requiring direct experimental validation.