IndraLab

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USP13 binds MYC. 20 / 21
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"The MYC-USP13 group also significantly reduced PTEN ubiquitination in comparison with control group in HCT116 cells ( xref )."
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"We showed a strong molecular association between USP13 and c-MYC, leading to the upregulation of squamous programs in murine and human lung cancer cells."
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"By coexpressing USP13‐Myc and Bcl‐XL‐Flag in HEK293T cells, we discovered that USP13 could be detected in Bcl‐XL immunoprecipitates after pull down by anti‐Flag beads ( Figure   xref )."
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"USP13 and FBXL14 interact with c-Myc in glioma cells."
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"However, overexpression of CLK3 in HCCC9810 cells promoted the binding of c-Myc to WT-USP13, not USP13 Y708F mutant (XREF_FIG)."
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"The interaction between c-Myc and USP13 or FBXL14 was validated in HEK293 cells coexpressing c-Myc and Flag tagged USP13 or FBXL14."
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"These results demonstrate that c-Myc interacts with USP13 and FBXL14 in glioma cells, indicating that deubiquitinase USP13 and the ubiquitin E3 ligase FBXL14 are potential regulators of c-Myc protein stability in GBM."
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"Computational modeling of structures predicted in ZDOCK and Pymol software showed that Y708 phosphorylation was necessary for the direct binding of USP13 to c-Myc (XREF_FIG)."
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"As USP13 is a deubiquitinase, the interaction between USP13 and c-Myc led us to hypothesize that USP13 may stabilize c-Myc protein in GSCs through deubiquitination."
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"To investigate whether USP13 mediated the deubiquitination of cohesin subunits, we cotransfected 293T cells with expression vectors for His-ubiquitin and Myc-USP13, purified ubiquitinated proteins by Ni-NTA affinity chromatography, and performed Western blot with antibodies to SMC3 and RAD21 ( xref A )."
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"Subsequently, to identify the binding site of USP13 on Beclin-1, we employed cells expressing one of three BECN1 deletion mutants alongside MYC–USP13 constructs for Co-IP assays."
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"We then examined the physiological significance of USP13 phosphorylation by CLK3 at Y708. xref indicates that CLK3 knockdown in HuCCT1 cells strongly impaired the interaction of USP13 with c-Myc."
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"Computational modeling of structures predicted in ZDOCK and Pymol software showed that Y708 phosphorylation was necessary for the direct binding of USP13 to c-Myc ( xref )."
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"Surprisingly, USP13 was found to be phosphorylated by CDC-like kinase 3 (CLK3), and this phosphorylation promotes the binding of USP13 to c-Myc, thus stabilizing c-Myc protein levels and enhancing its transcriptional activity in cholangiocarcinoma (CCA) [ xref ]."
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"Meanwhile, a gain of function somatic mutation Q607R was identified in CLK3 kinase domain, which induced USP13 Y708 phosphorylation and promoted USP13 binding to c-Myc."
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"As USP13 is a deubiquitinase, the interaction between USP13 and c-Myc led us to hypothesize that USP13 may stabilize c-Myc protein in GSCs through deubiquitination."
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"Moreover, phosphorylation of USP13 at Y708 by CDC-like kinase 3 (CLK3) can facilitate the interaction between USP13 and the proto-oncoprotein c-Myc, further suppressing tumorigenesis ( xref )."
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"In cholangiocarcinoma, TGF-β signaling triggers the phosphorylation of CLK3, a serine/threonine kinase that directly phosphorylates USP13 at Y708 and facilitates USP13 interaction with c-Myc ( xref ); in GSCs, USP13 can enhance the stability through deubiquitinating c-Myc, activating purine synthesis mediated by c-Myc and inducing the tumorigenesis of GSCs ( xref ); in hepatocellular carcinoma, knockdown of USP13 by shRNA can markedly downregulate c-Myc expression, resisting xenograft tumor growth of HCC ( xref )."
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