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AKT binds OTUD1. 16 / 16
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"We identified a peptide (OUN-36) derived from the OTUD1 N-terminus that binds to the Akt PH domain and disrupts its interaction with PIP3."
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"An in vitro pulldown assay with purified GST-OTUD1 and His-PH demonstrated that the Akt PH domain directly bound to OTUD1 ( Figures 3 D and S3 C)."
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"16 To confirm the identified protein interaction, we expressed both Akt and OTUD1 in HEK293T cells, and coimmunoprecipitation (Co-IP) clearly showed that OTUD1 bound to Akt ( Figure 1 B)."
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"As shown in Figure 1 D, purified OTUD1 bound to Akt."
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"33 Interestingly, our results indicated that OTUD1 binds to the Akt PH domain in a growth factor-independent manner."
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"Notably, the OTUD1 N-terminal intrinsically disordered region contains an abundance of proline (16.9%) and glycine (9.6%) residues, implying that this region is highly flexible, which may facilitate t[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Very recently, Fan et al. showed that OTUD1 binds AKT most strongly among 11 OTU family DUBs, and then suppresses its phosphorylation [24]."
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"9 We detected an interaction between OTUD1 and Akt in cells stimulated with EGF or insulin, which activated Akt signaling, and we found that the OTUD1-Akt interaction was not affected ( Figure S1 D)."
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"A 36-amino acid (aa) peptide (OUN-36) located in the OTUD1 N-terminal intrinsically disordered region is responsible for the interaction of OTUD1 with Akt."
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"Consistent with the above results, in the absence of this 36-aa peptide, the interaction between OTUD1 and Akt became nearly undetectable ( Figure 2 G)."
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"Co-IP showed that only the PH domain of Akt interacted with either OTUD1 or OUN-36 ( Figures 3 B and 3C)."
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"To identify possible protein interactions between OTU DUBs and Akt, we performed a pulldown-based screen and found that OTUD1 strongly binds to Akt and is capable of inhibiting Akt activation."
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"In this study, we identified a 36-aa peptide derived from OTUD1 N-terminal intrinsically disordered region that directly binds to Akt PH domain."
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"Meanwhile, we also found that AKT did not bind with OTUD1 in 786-O cells ( xref A)."
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"To explore whether OTU DUB family members interact with Akt, we carried out screening by performing a pulldown assay and found that OTUD1 strongly interacted with Akt ( Figure 1 A)."
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"Interestingly, the interactions between proteins with PH domain such as PDK1 or AGC kinase such as SGK1 and OUN-36 were not detected ( Figures S3 A and S3B), suggesting that OTUD1 36-aa motif specific[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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