Recombinant Human ATP5C1 protein

ATP5C1. also known as the gamma subunit of mitochondrial ATP synthase (Complex V), is a critical component of the oxidative phosphorylation (OXPHOS) machinery responsible for cellular energy production. This nuclear-encoded protein localizes to the mitochondrial inner membrane, where it forms part of the catalytic F1 domain of ATP synthase. The enzyme complex couples proton gradient-driven rotation of its transmembrane FO sector with ATP synthesis in the F1 domain through a mechanism involving conformational changes in the gamma subunit. As the central rotor stalk component, ATP5C1 plays a structural and functional role in coordinating energy transfer between FO and F1 domains.

Recombinant ATP5C1 protein is typically produced using heterologous expression systems (e.g., E. coli or mammalian cells) for biochemical and structural studies. Its production enables detailed investigation of ATP synthase assembly, enzyme kinetics, and proton transport mechanisms. Researchers utilize purified ATP5C1 to study mutations affecting mitochondrial function, particularly those linked to neuromuscular disorders and metabolic diseases. For instance, specific ATP5C1 variants have been associated with mitochondrial encephalopathy and ATP synthase deficiencies characterized by impaired cellular energy metabolism.

Recent studies highlight ATP5C1's potential role in cancer progression, as many tumors show altered ATP synthase expression patterns. The recombinant protein serves as a tool for developing inhibitors targeting cancer-specific ATP synthase isoforms. Additionally, ATP5C1 has been implicated in neurodegenerative conditions like Alzheimer's disease, where mitochondrial dysfunction contributes to pathogenesis. Structural analyses using recombinant protein help map interaction interfaces with regulatory proteins like IF1 (ATPase inhibitory factor 1), providing insights into metabolic regulation under hypoxic conditions. Current research focuses on understanding post-translational modifications of ATP5C1 and their impact on cellular adaptation to energy stress.