Phosphate (P_i) homeostasis is a tightly regulated process in all organisms. Dysfunction of P_i homeostasis leads to renal Fanconi syndrome in humans, severe growth retardation in plants, and lethality in microorganisms. To achieve a delicate balance between the biosynthetic requirements for P_i and the risks of excessive cytoplasmic P_i, unicellular organisms maintain important P_i stores in membrane-bound, acidocalcisome-like organelles in the form of inorganic polyphosphates (polyP). As the only known eukaryotic polyP synthetase, Saccharomyces cerevisiae vacuolar transporter chaperone (VTC) complex synthesizes polyP from adenosine triphosphate (ATP) and translocates polyP across the vacuolar membrane to maintain an intracellular P_i homeostasis. In this article, the latest progress on the structure and function of VTC complexes were reriewed from the aspects of structural characteristics, polyP synthesis, and polyP transport mechanism. The focus is on the recently published intact structural of VTC complexes and exploring the activation mechanism of VTC.