IndraLab

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STAMBPL1 activates mTORC1. 5 / 5
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"When leucine is sufficient, STAM-binding-protein-like 1 (STAMBPL) removes the ubiquitin chain on Sestrin2 and activates the mTORC1 signal [80]."
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"STAMBPL1 knockout significantly suppressed mTORC1 activity, anchorage-independent cell growth, and xenograft tumor growth ( Figures 5 F–5J and S8 C–S8J) in all three cell lines."
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"When overexpressed in cells, STAMBPL1 catalyzed the deubiquitination of Sestrin2 ( Figure 2 C) and promoted mTORC1 activation ( Figure 2 D)."
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"Accordingly, STAMBPL1(K405Rfs ∗ 21) showed higher interaction level with Sestrin2, even in the absence of amino acids or leucine ( Figures 6 B and S9 C), and activated mTORC1 signaling ( Figure 6 C)."
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"To further test if the catalytic activity of STAMBPL1 is required to modulate mTORC1 signaling, we mutated the water-activating Glu 292 (E292A) and the Zn 2+ -coordinating Asp 360 (D360A) residues in [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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