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USP36 binds MYC. 26 / 33
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"Myc-USP36 proteins were predominantly localized in nucleoli."
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"Hence, the interaction between USP36 and c-Myc in colon cancer cells was investigated to uncover the potential mechanism underlying the oncogenic effect of USP36."
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"To complement the USP36 RNAi experiments, we overexpressed myc-USP36 in HeLa cells."
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"Immunofluorescence analysis showed nucleolar localization of myc-USP36 ( Fig. 4 A)."
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"Interestingly, myc-USP36 remained in nucleoli throughout the CCCP treatment time course."
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"Besides, USP36 can interact with c-Myc and FBW7γ, then deubiquitinating c-Myc and counteracting the degradation mediated by FBW7γ ( Sun et al., 2015 )."
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"Myc-USP36 transfection did not affect Parkin translocation after treatment with CCCP for 2 h or mitochondrial elimination after 24 h ( Fig. 4 A)."
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"For example, as demonstrated by Sun and colleagues, USP36 could interact with and deubiquitinate c-Myc in nuclear, thus enhancing c-Myc signaling and regulating cell proliferation [ 10 ]."
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"The interaction between c-Myc and USP36 was mediated via Fbxw7γ, reminiscent of the ‘piggyback’ interaction of USP28/Fbw7/c-Myc described by Eilers and colleagues [89] , but this interaction was limit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"A recent published data indicated that USP36 could interact with and deubiquitinate c-Myc, thereby suppressing c-Myc degradation and promoting c-Myc signaling [ 10 ], and such mechanisms might be invo[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The Ni-NTA pull down of 6xHIS tagged ubiquitinated proteins revealed that USP30-HA expression severely reduced the poly-ubiquitination of mitochondrial Parkin substrates, whereas myc-USP36 expression [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Interestingly, Parkin itself was deubiquitinated after USP30-HA expression, but showed an increased poly-ubiquitination signal after myc-USP36 expression, even in unstressed cells (0 h CCCP)."
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"Myc-USP36 was found predominantly in the nucleolus throughout the time course of mitophagy ( Fig. 1 A, D; Figs."
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"The interaction between c-Myc and USP36 was mediated via Fbxw7γ, reminiscent of the ‘piggyback’ interaction of USP28/Fbw7/c-Myc described by Eilers and colleagues [89] , but this interaction was limit[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"A reduction of Parkin translocation to mitochondria was observed, while the re-introduction of overexpressed myc-USP36 wild type (WT) but not the catalytically inactive mutant (myc-USP36C131A) restore[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As shown in xref B , ectopic Myc-USP36 was coimmunoprecipitated with HA-survivin using an anti-HA antibody, and ectopic HA-survivin was coimmunoprecipitated with Myc-USP36 using an anti-Myc antibody."
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"In agreement with previous results, Myc-USP36 was associated with cIAP1 and survivin."
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"The plasmid pCMV-PARP1-3xFlag-WT (#111575) was procured from Addgene (Cambridge, MA, USA), Myc-USP36 and His-ubiqutin were supplied by Realgene, Nanjing, China."
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"To investigate USP36-binding proteins in cells, the HEK293T cells were transfected with Myc-USP36 or control vector and cultured for 24 h."
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"As shown in Fig. 3 F, Flag–PARP1 was coimmunoprecipitated with Myc-USP36 using an anti-Myc antibody."
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"Expectedly, Myc-USP36 was also coimmunoprecipitated with Flag–PARP1 using an anti-Flag antibody ( Fig. 3 G)."
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"In this study, we transfected wild-type USP36 (Myc-USP36 WT) or an inactivating mutant containing a point mutation in the catalytic site USP36 (Myc-USP36 C131A) into HEK293T cells or H9C2 cells."
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"USP36 interacts with and deubiquitinates c-Myc in cells and in vitro, leading to the stabilization of c-Myc."
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"To investigate whether USP36 regulates PARP1 levels through deubiquitination, we transfected HEK293T cells with His–ubiquitin and FLAG-PARP1, with Myc-USP36 WT or Myc-USP36 C131A overexpression."
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"We further show that USP36 itself is a c-Myc target gene, suggesting that USP36 and c-Myc form a positive feedback regulatory loop."
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"Both USP28 and USP36 can bind to c-MYC in cells, and deubiquitinize c-MYC, thereby modulating cancer cell growth and apoptosis (Popov et al., 2007; Sun et al., 2015)."
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