ATP6V1F

ATP6V1F, also known as V-ATPase subunit F, is a component of the vacuolar H+-ATPase (V-ATPase) enzyme complex. The V-ATPase is a multi-subunit enzyme complex responsible for acidifying intracellular compartments in eukaryotic cells. It utilizes the energy derived from ATP hydrolysis to pump protons (H+) across cellular membranes, thereby creating an electrochemical gradient. This gradient is crucial for a wide array of cellular processes including protein trafficking, receptor-mediated endocytosis, synaptic vesicle acidification, and bone resorption.

The V-ATPase complex is composed of two functional domains: the V1 domain, which is responsible for ATP hydrolysis, and the V0 domain, which mediates proton translocation. The V1 domain is peripheral and consists of eight subunits (A-H), while the V0 domain is integral to the membrane and consists of several subunits including a, d, c, c', and c". ATP6V1F is one of the subunits comprising the V1 domain.

Specifically, ATP6V1F is believed to play a structural role within the V1 domain, contributing to the proper assembly and stability of the complex. It interacts with other V1 subunits to facilitate ATP binding and hydrolysis. Mutations in genes encoding V-ATPase subunits, including ATP6V1F, have been linked to various human diseases, including distal renal tubular acidosis (dRTA), osteopetrosis, and neurodegenerative disorders, underscoring the importance of this enzyme complex and its constituent subunits in maintaining cellular homeostasis. While the exact function of ATP6V1F is still under investigation, research suggests it contributes to the efficiency and regulation of the V-ATPase pump.