When vesicles containing Hantavirus matured into acidic endosomes, Gn dissociated under an acidic environment, exposing Gc's autophosphorylation domains. Gc's autophosphorylation domain initiated and completed autophosphorylation. Gc autophosphorylation activated the C2 domain. The C2 domain facilitated the conformational shift of Gc necessary for activation of the phosphatase domain. Then Gc had the activity of PTEN-like. Under conditions of PTEN-like activity, Gc was bound to the endosomal membrane. Gc's phosphatase domain phosphorylated PI P3 on the endosomal membrane following its insertion into the membrane. Then conversion of PI P3 to PI(4,5)P2. PI(4,5)P2 bound to the N-terminus of Gc, allowing the tetramer-shaped Gc to adhere to the endosomal membrane fully. In the endosomal membrane, Hantavirus generated fusion holes. A slight coating of hydrated calcium ions may exist at the point of contact between the Gc tetramer and the endosomal membrane. The Gc tetramer was a phospholipid flippase. It drained water from the hydrated calcium ion layer, quickly fliped phospholipid and spliced membranes to form the fusion hole. Because phosphorylation of PI P3 directly triggered the breakdown of the Gc tetramer on the inner membrane, similar to PTEN breakdown. The expansion of the fusion hole speeded the fusion of the viral membrane and the endosomal membrane. The virus's intracellular material was swiftly ejected into the cytoplasm.