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Statements

STAMBPL1 binds SESN2. 16 / 16
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"The results indicated that in the SMAD3 overexpression group, the binding of Sestrin2 to STAMBPL1 increased, whereas in the SMAD3 knockdown group, the binding of Sestrin2 to RNF167 was significantly enhanced (Fig.  xref C, D)."
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"Inhibiting the interaction between STAMBPL1 and Sestrin2 thereby inactivating mTORC1 using a cell-permeable peptide could be a potential treatment approach for gastric and colorectal cancers [ xref ]."
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"The binding of RNF167 and STAMBPL1 to Sestrin2 is not mutually exclusive, as the interaction of one protein with Sestrin2 was not affected by deficiency or overexpression of the other protein ( Figure[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Importantly, we demonstrated that disrupting the STAMBPL1-Sestrin2 interaction with a cell-penetrating peptide might serve as a potential strategy for colon cancer therapy."
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"Moreover, a cell-permeable peptide that blocks STAMBPL1-Sestrin2 interaction suppresses mTOR signaling and anchorage-independent cell growth of human colon cancer cells."
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"Inhibiting the interaction between STAMBPL1 and Sestrin2 thereby inactivating mTORC1 using a cell-permeable peptide could be a potential treatment approach for gastric and colorectal cancers [141]."
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"Next, we tested whether a cell-permeable peptide disrupting STAMBPL1-Sestrin2 interaction may suppress cancer development."
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"Deleting the USP8_dimer domain or the linker region between the USP8_dimer domain and the JAB domain (UJ_linker) suppressed STAMBPL1-Sestrin2 interaction ( Figures S10 A and S10B)."
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"The binding of leucine may alter Sestrin2 conformation, promoting Sestrin2-STAMBPL1 interaction and resulting in removal of the ubiquitin chain."
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"Therefore, disrupting the STAMBPL1-Sestrin2 interaction with a cell-permeable peptide may be a promising therapeutic strategy for gastric and colorectal cancers."
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"A cell-permeable peptide disrupting STAMBPL1-Sestrin2 interaction can inhibit mTORC1 signaling and suppress colon cancer cell growth ( Figure 7 F)."
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"In contrast, changes in arginine levels did not affect RNF167-Sestrin2 or STAMBPL1-Sestrin2 interaction ( Figures S4 C and S4D)."
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"Supplementation of His-Sestrin2 purified from bacteria with leucine, but not arginine, significantly affected RNF167-Sestrin2 and STAMBPL1-Sestrin2 interactions ( Figures 3 D and 3E)."
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"Consistent with the role of leucine in modulating the interaction of Sestrin2 with E3 ligase RNF167 and DUB STAMBPL1, deficiency of RNF167 or STAMBPL1 affected mTORC1 activity in response to changes i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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