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USP13 binds FlaG. 20 / 20
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"Forced expression of FLAG-USP13 partially reversed the U0126-caused vimentin reduction ( Figures 4 H and S6 D)."
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"Results showed that when HA-Ub-K48 and FLAG-USP13 were co-transfected, the ubiquitination level of MYC-HIF-1α was markedly reduced."
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"However, when K48 was mutated to arginine (K48R), the ubiquitination level of HIF-1α remained unchanged despite the presence of FLAG-USP13."
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"As expected, substitution of FLAG-USP13 with FLAG-USP13-AE resulted in a pronounced increase in HIF-1α ubiquitination, closely resembling the levels observed in the absence of FLAG-USP13 (Fig.  xref G)."
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"FLAG-USP13 was transfected into 293 T cells in a gradient manner, and the protein level of HIF-1α was assessed using Western blot analysis."
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"We first performed co-immunoprecipitation assays to confirm the interaction between USP13 and Mcl-1 by transfecting HEK293T cells with FLAG-USP13 and V5-hMcl-1."
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"We also observed that re-expression of wild-type (WT) FLAG-USP13, but not catalytically inactive mutant (C345A) USP13, in H1299 USP13 -KO cells could rescue invasive phenotype in vitro ( Figure S1 H)."
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"Immunoprecipitation with anti-FLAG antibody demonstrated that FLAG-USP13 interacted with over-expressed Mcl-1 (Fig. xref )."
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"Consistent with in vitro transwell assay, we observed that depletion of USP13 significantly reduced the number of metastatic nodules, whereas re-expression of WT but not C345A FLAG-USP13 increased the[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"HEK293T cells were transfected with FLAG-USP13, V5-Mcl-1 and HA-Ubiquitin, and anti-V5 immunoprecipitates were probed for the level of ubiquitination using the HA-antibody."
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"To explore the mechanism underlying the pro-metastatic effect of USP13, we analyzed the expression of key proteins involved in cancer metastasis, including Zeb1, E-cadherin, N-cadherin, Snail, Twist, [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The decrease in HIF-1α protein level caused by USP13 knockout was reversed upon reintroduction of FLAG-USP13 (Fig.  xref L)."
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"Meanwhile, we detected that vimentin mRNA level was also decreased in USP13 -KO cells and increased in USP13 -KO cells ectopically expressing FLAG-USP13 ( Figures S3 C and S3D)."
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"24 To explore the molecular mechanism by which USP13 promotes vimentin expression, immunoprecipitated complex of FLAG-USP13 was subjected to mass spectrometry (MS) analysis to identify the potential U[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Given that β-catenin is an important regulator in cancer metastasis, 32 we then confirmed USP13/β-catenin interaction through immunoprecipitation (IP) assay in H1299 cells co-transfected with FLAG-USP[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"To map the interacting domains of HIF-1α and USP13, truncated MYC-HIF-1α and FLAG-USP13 variants were transfected into 293 T cells."
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"We found that endogenous TopBP1 co-immunoprecipitated with FLAG-USP13 ( xref )."
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"In contrast, when K63 was mutated (K63R), FLAG-USP13 expression significantly reduced HIF-1α ubiquitination, as K48-linked ubiquitination remained intact (Fig.  xref I)."
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"As shown in the Fig.  xref J, when ubiquitin mutants targeting alternative lysine residues (K6, K11, K27, K29, K33) were transfected, the ubiquitination level of HIF-1α remained unchanged, in the presence of FLAG-USP13."
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"We observed that addition of His6-USP10, but not His6-USP13, reduced the amount of HA-Ub-conjugated FLAG-LC3B ( xref , C and D ), consistent with USP10 specifically catalyzing the deubiquitination of LC3B. Finally, we found that GFP-tagged LC3B (GFP-LC3B) co-immunoprecipitated with FLAG-USP10 but not FLAG-USP13 ( xref E )."
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