Necroptosis, a programmed cell death mechanism distinct from apoptosis, has been increasingly recognized for its role in various pathological conditions. While initially associated with cell death, recent research has shown that key necroptotic mediators, such as receptor-interacting protein kinases (RIPKs) and mixed lineage kinase domain-like protein (MLKL), also play roles in metabolic regulation, including energy metabolism, glucose homeostasis, and lipid metabolism. Dysregulated necroptosis has been implicated in metabolic diseases like obesity, diabetes, metabolic dysfunction-associated steatotic liver disease (MASLD), and alcohol-associated liver disease (ALD), contributing to chronic inflammation and tissue damage. This review explores the multifaceted role of necroptosis in metabolic diseases, including both cell death and extra-necroptotic functions. Understanding this interplay is crucial for developing targeted therapeutic strategies for diseases lacking effective treatments. Necroptosis is characterized by the activation of RIPKs and the subsequent phosphorylation and activation of MLKL, leading to plasma membrane rupture and release of intracellular contents. The classical necroptotic pathway involves the activation of death receptors, such as tumor necrosis factor receptor (TNFR) 1, Fas/CD95, and TRAIL receptors, leading to the formation of a membrane signaling complex. This complex includes components like TRADD, FADD, RIP1, TRAF2/5, and cIAP1/2, which determine whether the cell will undergo pro-survival or death pathways. When caspase-8 is inhibited, RIP1 can autophosphorylate and bind with RIP3, leading to the formation of the necrosome and the phosphorylation and oligomerization of MLKL, which executes necroptosis. Non-classical necroptotic pathways involve other receptors and intracellular sensors, such as toll-like receptors (TLR3 and TLR4) and ZBP1, which can initiate necroptosis through different pathways. Post-translational modifications, including phosphorylation and ubiquitination, regulate the necroptotic pathway. These modifications influence the activity of RIP1, RIP3, and MLKL, affecting cell survival and death. For example, phosphorylation of RIP1 at S166 is critical for regulating RIPK1 kinase-dependent cell death and inflammation. Ubiquitination of RIP1 plays a role in TNF-α-mediated cell survival and death signaling. RIP3 is involved in various metabolic processes, including lipid metabolism, and its expression is increased in conditions like MASH and ALD. RIP3 deficiency can protect against ethanol-induced liver damage, but its role in different dietary conditions can vary. MLKL is also involved in lipid metabolism and has non-canonical functions, such as modulating lipid uptake, transport, and metabolism. MLKL can translocate to various intracellular compartments, including mitochondria,Necroptosis, a programmed cell death mechanism distinct from apoptosis, has been increasingly recognized for its role in various pathological conditions. While initially associated with cell death, recent research has shown that key necroptotic mediators, such as receptor-interacting protein kinases (RIPKs) and mixed lineage kinase domain-like protein (MLKL), also play roles in metabolic regulation, including energy metabolism, glucose homeostasis, and lipid metabolism. Dysregulated necroptosis has been implicated in metabolic diseases like obesity, diabetes, metabolic dysfunction-associated steatotic liver disease (MASLD), and alcohol-associated liver disease (ALD), contributing to chronic inflammation and tissue damage. This review explores the multifaceted role of necroptosis in metabolic diseases, including both cell death and extra-necroptotic functions. Understanding this interplay is crucial for developing targeted therapeutic strategies for diseases lacking effective treatments. Necroptosis is characterized by the activation of RIPKs and the subsequent phosphorylation and activation of MLKL, leading to plasma membrane rupture and release of intracellular contents. The classical necroptotic pathway involves the activation of death receptors, such as tumor necrosis factor receptor (TNFR) 1, Fas/CD95, and TRAIL receptors, leading to the formation of a membrane signaling complex. This complex includes components like TRADD, FADD, RIP1, TRAF2/5, and cIAP1/2, which determine whether the cell will undergo pro-survival or death pathways. When caspase-8 is inhibited, RIP1 can autophosphorylate and bind with RIP3, leading to the formation of the necrosome and the phosphorylation and oligomerization of MLKL, which executes necroptosis. Non-classical necroptotic pathways involve other receptors and intracellular sensors, such as toll-like receptors (TLR3 and TLR4) and ZBP1, which can initiate necroptosis through different pathways. Post-translational modifications, including phosphorylation and ubiquitination, regulate the necroptotic pathway. These modifications influence the activity of RIP1, RIP3, and MLKL, affecting cell survival and death. For example, phosphorylation of RIP1 at S166 is critical for regulating RIPK1 kinase-dependent cell death and inflammation. Ubiquitination of RIP1 plays a role in TNF-α-mediated cell survival and death signaling. RIP3 is involved in various metabolic processes, including lipid metabolism, and its expression is increased in conditions like MASH and ALD. RIP3 deficiency can protect against ethanol-induced liver damage, but its role in different dietary conditions can vary. MLKL is also involved in lipid metabolism and has non-canonical functions, such as modulating lipid uptake, transport, and metabolism. MLKL can translocate to various intracellular compartments, including mitochondria,