Fig. 1

The mTORC1 and mTORC2 complex. The FKBP12-rapamycin complex binds to the FK506-binding protein 12 and inhibits mTORC1 by blocking its association with the FRB domain. This leads to steric hindrance and prevents the activation of mTORC1. On the other hand, mTORC2 is resistant to rapamycin due to the presence of rictor and msin1, which block the binding of the FKBP12-rapamycin complex to the FRB domain of mTORC2. In the mTORC1 complex, raptor plays a crucial role in promoting the phosphorylation of various downstream targets. mlst8 stabilizes the mTORC1 complex, whereas deptor negatively regulates its activity. pras40 also interacts with mTORC1. In the mTORC2 complex, rictor is an essential component that helps stabilize the complex while msin1 contributes to its regulation. This figure provides insight into the structural components and interactions within mTORC1 and mTORC2 complexes, highlighting their sensitivity or insensitivity to the FKBP12-rapamycin complex and the respective roles of key proteins. raptor, regulatory-associated protein of TOR; mlst8, mammalian lethal with sec-13 protein 8; deptor, DEP domain–containing mTOR interacting protein; pras40, proline-rich Akt substrate of 40kD; rictor, rapamycin-insensitive companion of mTOR; msin1, stress-activated protein kinase interacting protein 1