IndraLab

Statements

USP48 is sumoylated. 11 / 11
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"Our findings demonstrated that HDAC4 and HDAC7 promoted the SUMOylation of USP48, while SENP5 cleaved it."
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"Although we failed to identify a conserved SIM motif in HMGA2, our findings demonstrated that the SUMOylated USP48 could still strongly interact with HMGA2, thereby enhancing the affinity of USP48 for ubiquitin chains and augmenting its DUB activity."
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"We hypothesize that the SUMOylation of USP48 may interact with a non-classically conserved SIM motif (V-V-Q-K) in the HMGA2 protein, or induce conformational changes in USP48 to better accommodate the HMGA2 protein xref ."
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"In CRC cells, it was observed that endogenous USP48 underwent poly-SUMOylation ( xref D and E)."
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"Co-expression of HDAC4 or HDAC7 facilitated the SUMOylation of USP48 protein ( xref H), while SENP5 inhibited the SUMOylation of USP48 protein ( xref I and J)."
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"Furthermore, SUMOylation of USP48 significantly enhanced its ability to stabilize HMGA2 and promote CRC cell invasion and metastasis in an HMGA2-dependent manner."
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"Additionally, substitution of the putative SUMOylation site Lys258 (USP48-K258R) with arginine resulted in a near-complete abrogation of USP48 protein SUMOylation ( xref L)."
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"These findings suggest that HDAC4/7 and SENP5 play a role in the dynamic regulation of USP48 protein SUMOylation, with Lys258 identified as a potential site for this modification."
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"We conducted PLA experiments to determine the subcellular localization of SUMOylated USP48."
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"Next, we investigated the role of USP48 SUMOylation in driving invasive metastasis in CRC."
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"The findings suggest that SUMOylation of USP48 significantly enhances its ability to stabilize HMGA2 and promote CRC invasion and metastasis in a HMGA2-dependent manner."
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