Our results reveal a structural model for the mechanism of the Rag GTPases in TORC1 activation and amino acid signaling.Ĭancer Institute, Shanghai Cancer Center, Department of Oncology, Shanghai Medical College, Fudan University, Shanghai 200032, China. Dozens of free watch faces2 are available to download from the App for you to choose from and switch. The dimerized C-terminal domains of RagA-RagC display a remarkable structural similarity to MP1/p14, which is in a complex with lysosome membrane protein p18, and directly interact with p18, therefore recruiting mTORC1 to the lysosome for activation by Rheb. In particular, the switch regions of the G domain in RagA are indispensible for interaction with raptor, and hence TORC1 activation. Structure-guided functional analyses of RagA-RagC, the human homologs of Gtr1p-Gtr2p, show that both G domains (N-terminal GTPase domains) and dimerization are important for raptor binding. The heterodimeric GTPases reveal a pseudo-twofold symmetric organization. Here we present the crystal structure of the Gtr1p-Gtr2p complex, the Rag homologs from Saccharomyces cerevisiae, at 2.8 Å resolution. The Rag GTPases play an essential role in relaying amino acid signals to TORC1 activation through direct interaction with raptor and recruitment of the TORC1 complex to lysosomes. 1 Manual start by press keys E and si mul ta ne ous ly. The target of rapamycin (TOR) complex 1 (TORC1) is a central cell growth regulator in response to a wide array of signals. a Safety switch 10V i mA/Pt always in position left or right. Biologically Interesting Molecule Reference Dictionary (BIRD).
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