Target Of Rapamycin (TOR) kinase was initially discovered in yeast and is highly conserved across eukaryotes. TOR kinase operates through two distinct complexes, TORC1 and TORC2, with specific roles and locations in cells. While TORC1 is inhibited by rapamycin and well-studied, TORC2 remains less understood.

The study aimed to resolve the high-resolution structure of TORC2 and shed light on its assembly and regulation. I successfully determined the structure of TORC2 at 2.34 Å resolution, including the previously unresolved component Bit61. We also characterized the substrate-bound and autoinhibited TORC2 structures, revealing the inhibitory role of the Avo1 PH domain.

Additionally, we discovered co-purifying eisosome filaments during TORC2 purification. The structure of these filaments was resolved, demonstrating their association with the plasma membrane and revealing insights into the assembly of Pil1 lattice within the eisosomes. This discovery provides a model for investigating the native composition and morphology of the plasma membrane.