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USP28 binds FBXW7. 43 / 44
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"Loss of the USP28-FBW7 complex."
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"Past investigations revealed that although many FBW7 domains, including WD40, promoted FBW7’s binding to USP28, the amino terminus of FBW7 contributed to the interaction of FBW7, c-Myc and USP28 [5, 29]."
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"Therefore, the loss of the USP28-FBW7 complex could stabilize BRAF to potentiate activating downstream MAPK pathway, promoting the therapeutic resistance to BRAF-targeted therapy."
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"Several mechanisms of intrinsic resistance have been described among whom loss of PTEN, cyclin D1 amplification, loss of NF1, RAC1 P29S mutation, HGF secretion, MAP3K8 overexpression, loss of the USP28–FBW7 complex, low levels of CD8 tumor-infiltrating T cells and increased expression of the immune inhibitory molecule PD-L1 ( xref – xref )."
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"Collectively, the loss of USP28-FBW7 complex-mediated BRAF degradation stimulates the intrinsic resistance to MAPK inhibition targeted therapy in melanoma [ xref , xref ]."
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"Discovery of an analog of the Fbw7 and Usp28 complex in Drosophila demonstrates that such complexes represent an evolutionary conserved regulatory paradigm (Li et al., 2013)."
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"In case of the Fbw7 and Usp28 complex, we suggest that wiring control of the ligase and its substrates to a single DUB ensures that stabilization of proto-oncoproteins during homeostatic processes occ[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Due to mutations in RAC1, loss of PTEN, NF1, CCND1, USP28-FBW7 complex, COT overexpression, and CCND1 amplification, the BRAF kinase enzyme developed resistance over the commercially available BRAF inhibitors."
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"USP28 can bind to FBXW7 and inhibit ubiquitination modification of c-Myc by the latter, thus increasing the protein stability of c-Myc ( xref )."
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"Past investigations revealed that although many FBW7 domains, including WD40, promoted FBW7’s binding to USP28, the amino terminus of FBW7 contributed to the interaction of FBW7, c-Myc and USP28 [ xref , xref ]."
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"Genetic alterations, including loss of PTEN , amplification of CCND1 , loss of NF1 , RAC mutations, and loss of the USP28-FBW7 complex, have been identified in the development of intrinsic resistance."
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"We decided to focus our attention on USP28, as USP28 forms a complex with FBW7, a protein recently described to be mutated in melanoma."
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"USP28 also interacted with FBW7 under physiological conditions, as seen by endogenous FBW7 coimmunoprecipitating with endogenous USP28."
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"One interesting corollary of these findings was that an alternative to the ‘piggyback’ model of USP28 binding to substrates via Fbw7 must be acting in Fbw7-deleted animals."
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"Usp28 preferentially binds the Fbw7α isoform, whereas Usp36 selectively associates with Fbw7γ and both DUBs stabilize Myc."
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"Pulldown experiments using c-Myc peptides showed that USP28 and Fbw7 bind to the phosphorylated CPD motif; however, USP28 only bound to non-phosphorylated peptide in the absence of Fbw7 [91] ."
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"USP28 also binds the E3 ubiquitin ligase FBW7 to stabilize MYC and promote cell proliferation [33] ( Fig. 3 a)."
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"In unstressed cells, Usp28 forms a complex with Fbw7 and antagonizes substrate ubiquitination, whereas after DNA damage this complex dissociates, promoting Fbw7-dependent substrate degradation ( Popov[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Next, to study the effect of FBW7 and USP28 complex on BRAF ubiquitination, we cotransfected BRAF with either wild-type FBW7 or FBW7 (R505L)-binding mutant and analyzed endogenous BRAF ubiquitination levels."
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"Interestingly, the frequency of coalterations between USP28 and FBW7 is low (0.05%; 2/39) indicating that nearly 13% (37/287) of all melanoma patients contain mutations within the FBW7 and USP28 complex."
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"However, the functional significance of the USP28-FBXW7 partnership in maintaining SOX9 stability remains unexplored."
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"31 In another similar study, cross‐linked ORF in circFBXW7, driven by the IRES, was found to encode a new 21‐kDa protein called FBXW7‐185aa.61 FBXW7‐185aa can bind with USP28 to prevent USP28 binding with FBXW7α mRNA, thereby reducing the half‐life of c‐Myc and inhibiting proliferation and cell cycle progression, significantly inhibiting glioma progression (Figure 3C).61 5."
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"USP28 binds to substrates such as c-MYC, c-JUN, and NOTCH1 through interaction with FBXW7, and it stabilizes these proteins by reversing their ubiquitylation catalyzed by SCF FBXW7 ."
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"Additionally, USP28 forms complex with FBXW7 for binding to its catalytic substrate Ubiquitin ( Popov, Wanzel et al. 2007 )."
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"In unstressed cells, USP28 forms a complex with FBXW7 and antagonizes substrate ubiquitination, however, after DNA damage this complex dissociates promoting FBXW7-dependent substrate degradation []."
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"USP28 also binds the E3 ubiquitin ligase FBW7 to stabilize MYC and promote cell proliferation [33] ( Fig. 3 a)."
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"ChemMine Tools was used for performing structural clustering of the best scoring ligands from both sets of results obtained in our study i.e. Ub binding region of USP28 and FBXW7 binding region of USP[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Though ZDOCK and ClusPro gave different binding conformation of FBXW7 to the same UCID region of USP28, Pepsite2 validated that WD repeat region of FBXW7 binds to USP28 which was predicted by ZDOCK ( [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Though ZDOCK and ClusPro gave different binding conformation of FBXW7 to the same UCID region of USP28, Pepsite2 validated that WD repeat region of FBXW7 binds to USP28 which was predicted by ZDOCK ( [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Due to mutations in RAC1, loss of PTEN, NF1, CCND1, USP28-FBW7 complex, COT overexpression, and CCND1 amplification, the BRAF kinase enzyme developed resistance over the commercially available BRAF inhibitors."
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"Thus, FBW7-USP28 seems to work together to maintain the homeostasis of these proteins ( xref )."
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"The protein FBXW7-185aa functions as a tumor suppressor by competitively binding with USP28, and preventing USP28 binding to FBXW7α, subsequently inhibiting USP28-induced c-myc stabilization."
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"For example, USP28 and USP36 interact with FBW7 and reverse FBW7-mediated c-Myc degradation ( Popov et al., 2007 ; Sun et al., 2015 )."
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"Usp28 binds to Fbw7, and Usp28 was shown to be recruited to c-Myc protein indirectly through Fbw7 (the “piggyback” model) ( xref )."
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"Previous work has shown that Usp28 interacts with its substrates via binding to Fbw7 ( xref )."
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"Despite its initial success, resistance to BRAF inhibitors such as dabrafenib has emerged because of various factors, such as loss of PTEN, NF1, or USP28-FBW7, CCND1 amplification, COT overexpression, and mutations in RAC1 [ xref ]."
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"We decided to focus our attention on USP28, as USP28 forms a complex with FBW7, a protein recently described to be mutated in melanoma ( xref ; xref )."
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"USP28 also interacted with FBW7 under physiological conditions, as seen by endogenous FBW7 coimmunoprecipitating with endogenous USP28 (Fig. S2 H)."
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"These data suggest that the unphosphorylated degron motif can mediate Usp28 binding in the absence of Fbw7 ( xref )."
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"Meanwhile, the activity of FBXW7 can be antagonized by USP28, which binds directly to FBXW7 [24, 25]."
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"Alternatively, USP21 could be acting directly to deubiquitylate the substrates of the cullin RING ligase, in an analogous fashion to USP28, which associates with the cullin-1-adapter FBW7 to deubiquitylate a range of substrates, including MYC ( xref )."
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"Studies have identified the molecular mechanisms responsible for the intrinsic resistance include loss of PTEN , loss of NF1, CCND1 amplification, COT overexpression, mutations in RAC1 , and loss of the USP28-FBW7 complex [ xref , xref – xref ]."
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"USP28 interacts with and deubiquitinates FBW7 leading to the stability of FBW7 and consequently promoting degradation of FBW7 substrates."
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