IndraLab
Statements
reach
"In fact, it was subsequently found that USP28 binds to MYC at the same motif recognized by Fbw7, but only when it is unphosphorylated, and promotes deubiquitination of MYC in the absence of Fbw7.104 Moreover, it has been reported that USP28 dissociates from Fbw7α in response to DNA damage, allowing MYC to be degraded by Fbw7α.105 Adding another layer of complexity in regulating MYC, USP28 was reported to control the stability of Fbw7 by antagonizing its auto-ubiquitination and degradation in specific tissues such as lung, pancreas and liver, leading to destabilization of Fbw7 targets and to dose-dependent effects in Usp28 knockout mice."
sparser
"Among them, USP28 binds to Myc through an interaction with nucleoplasmic FBW7α, which is essential in breast and colon tumor cell proliferation [ xref , xref ], and USP36 binds to nucleolar Fbw7γ and controls the nucleolar degradation pathway of c-Myc in lung and breast cancer cells [ xref , xref ]."
reach
"Lanatoside C inhibited Wnt and beta-catenin signaling with downregulation of c-Myc, while overexpression of c-Myc reversed the anti-tumor effect of lanatoside C, confirming that c-Myc is a key drug target of lanatoside C. Furthermore, we discovered that lanatoside C prompted c-Myc degradation in proteasome-ubiquitin pathway with attenuating the binding of USP28 to c-Myc."
sparser
"In fact, it was subsequently found that USP28 binds to MYC at the same motif recognized by Fbw7, but only when it is unphosphorylated, and promotes deubiquitination of MYC in the absence of Fbw7. xref Moreover, it has been reported that USP28 dissociates from Fbw7α in response to DNA damage, allowing MYC to be degraded by Fbw7α. xref Adding another layer of complexity in regulating MYC, USP28 was reported to control the stability of Fbw7 by antagonizing its auto-ubiquitination and degradation in specific tissues such as lung, pancreas and liver, leading to destabilization of Fbw7 targets and to dose-dependent effects in Usp28 knockout mice."
sparser
"However, our finding shows that down-regulation of USP28 in BR cells attenuates c-Myc stability in a phosphorylation (Thr58/Ser62) site-independent manner, which is in agreement with other studies supporting that USP28 can directly bind to c-Myc in the absence of F-box protein Fbw7 [ xref ]."
sparser
"Recent studies showed that USP28 was involved in cancer-related pathways, and regulated physiological homeostasis of ubiquitination process, DNA-damage response, and cell cycle during genotoxic stress, which suggested that USP28 could be a promising target for cancer therapy. xref USP28 required for Myc function was screened. xref USP28 bound to Myc through an interaction with Fbw7α, and catalyzed the deubiquitination of Myc, thereby promoting its stabilization and contributing to tumor cell growth in colon and breast cancers. xref , xref USP28 can also bind to and deubiquitinate some proteins involved in DNA-damage pathways."
reach
"However, our finding shows that down-regulation of USP28 in BR cells attenuates c-Myc stability in a phosphorylation (Thr58 and Ser62) site independent manner, which is in agreement with other studies supporting that USP28 can directly bind to c-Myc in the absence of F-box protein Fbw7 [XREF_BIBR]."
sparser
"In addition, lanatoside C, a cardiac glycoside, has been shown to reduce MYC levels and suppress gastric cancer cell proliferation by inhibiting USP28 binding to MYC, thereby destabilizing MYC, although it remains to be determined whether lanatoside C directly targets USP28 ( xref )."
reach
"Among them, USP28 binds to Myc through an interaction with nucleoplasmic FBW7α, which is essential in breast and colon tumor cell proliferation [139,140], and USP36 binds to nucleolar Fbw7γ and controls the nucleolar degradation pathway of c-Myc in lung and breast cancer cells [141,142]."