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Structural basis for TORC2 activation
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DOI：10.1016/j.molcel.2026.03.022.png)
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Abstract
En 中文
• High-resolution cryo-EM structure of endogenous TORC2 • The PH domain of Avo1 inserts into the catalytic cleft to regulate kinase activity • Binding of the Avo1 PH domain to PI(4,5)P2 is required for activation • Activation of TORC2 involves structural rearrangements induced by signaling lipids
Keywords:
target of rapamycin complex 2
TOR signaling
cryo-electron microscopy
cell growth
phosphoinositides
membrane mechanotransduction