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USP4 binds HDAC2. 31 / 35
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"We found that TRPS1 scaffolding recruits and enhances interaction between USP4 and HDAC2 leading to HDAC2 de-ubiquitination and H4K16 deacetylation."
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"Furthermore, we sought to determine whether USP4 interacts with HDAC2 in vivo ."
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"These observations indicated that GATA-zinc finger domain of TRPS1 was essential for its interactions with HDAC2 and USP4."
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"We further verified that TRPS1 functioned as a scaffold protein for the complex formation of TRPS1-USP4-HDAC2 and was responsible for the reduction of HDAC2 ubiquitination level by facilitating interaction between USP4 and HDAC2."
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"USP4 's interaction with HDAC2 likely also emerged after WGD as a small region of USP4 (a.a. 188-302), which encompasses its unique alternatively spliced exon, interacts with this HDAC1 derived ohnolog."
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"It appeared that both TRPS1 and USP4 interacted with and stabilized HDAC2 in a UDPD-dependent fashion."
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"The results indicated that N-terminal or C-terminal domains of TRPS1 together with the GATA domain were sufficient to interact with HDAC2 and USP4 while neither TRPS1 N-terminal or C-terminal domain alone interacted with HDAC2 and USP4 (Fig. xref )."
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"USP4’s interaction with HDAC2 likely also emerged after WGD as a small region of USP4 (a."
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No evidence text available
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"We found that the interaction between endogenous USP4 and HDAC2 did not change after etoposide and TNFalpha treatment (XREF_SUPPLEMENTARY)."
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"We found that TRPS1 scaffolding recruits and enhances interaction between USP4 and HDAC2 leading to HDAC2 de-ubiquitination and H4K16 deacetylation."
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"Our results indicated that the GATA domain of TRPS1 alone was unable to interact with HDAC2 and USP4 (Fig. xref )."
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"Remarkably, the interaction between endogenous USP4 and HDAC2 is significantly decreased upon VPA treatment.( xref )."
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"We found that the interaction between endogenous USP4 and HDAC2 did not change after etoposide and TNFα treatment ( xref )."
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"These results reveal that USP4 protein directly binds to HDAC2 in the nucleus."
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"These results reveal that USP4 protein directly binds to HDAC2 in the nucleus."
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"Previous studies have shown that the histone deacetylase inhibitor VPA could induce proteasomal degradation of HDAC2. xref We detected the interaction between USP4 and HDAC2 after treatment with VPA."
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"Strong association of exogenous Myc-tagged USP4 with Flag-tagged HDAC2 was detected ( xref )."
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"Besides, the direct interaction between HDAC2 and USP4 was performed by the glutathione S-transferase (GST) pull-down assay."
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No evidence text available
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"We further verified that TRPS1 functioned as a scaffold protein for the complex formation of TRPS1-USP4-HDAC2 and was responsible for the reduction of HDAC2 ubiquitination level by facilitating interaction between USP4 and HDAC2."
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"Furthermore, we sought to determine whether USP4 interacts with HDAC2 in vivo."
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"It has recently been reported that USP4 directly interacts and de-ubiquitinates HDAC2 resulting in its stability in colon cancer cells [22]."
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"Remarkably, the interaction between endogenous USP4 and HDAC2 is significantly decreased upon VPA treatment."
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"29 We detected the interaction between USP4 and HDAC2 after treatment with VPA."
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"To further confirm the interaction between TRPS1, USP4, and HDAC2, we generated serial TRPS1 truncates based on the domain structure of TRPS1 consisting of an N-terminal domain and GATA and C-terminal domains (Fig. 3f)."
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"Besides, the direct interaction between HDAC2 and USP4 was performed by the glutathione S-transferase (GST) pull-down assay."
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"To test whether the TRPS1 GATA domain alone was sufficient to interact with USP4 or HDAC2 or both, we carried out Co-IP experiments in HEK293T cells with ectopic overexpression of TRPS1-GATA truncate containing only the GATA-zinc finger domain."
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"If the USP4–HDAC2 interaction enhances HDAC2 stability, then human tumors overexpressing USP4 protein might also overexpress HDAC2."
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"We hypothesized that TRPS1, USP4, and HDAC2 formed a complex, used Co-IP to test this notion, and found that TRPS1 co-immunoprecipitated with USP4 and HDAC2 (Fig. 3a, b)."
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