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Fig. 3 | Breast Cancer Research

Fig. 3

From: Tricho-rhino-phalangeal syndrome 1 protein functions as a scaffold required for ubiquitin-specific protease 4-directed histone deacetylase 2 de-ubiquitination and tumor growth

Fig. 3

Tricho-rhino-phalangeal syndrome 1 (TRPS1) transcription factor recruits ubiquitin-specific protease 4 (USP4) and histone deacetylase 2 (HDAC2) to form a complex in which HDAC2 is de-ubiquitinated by USP4. MCF7 (a) and T47D (b) show co-immunoprecipitation (Co-IP) of TRPS1, USP4 and HDAC2. MCF7 (c) and T47D (d) exhibit decreased HDAC2 protein levels upon silencing of USP4. e Co-IP analysis of the interaction between TRPS1, USP4, and HDAC2 in HEK293T cells with ectopic overexpression of Flag-TRPS1, Flag-USP4, and Myc-HDAC2 using anti-Myc antibody. f Domain structures of TRPS1 and its truncation mutants. g Co-IP analysis of the interaction between truncation mutants of TRPS1 and USP4 and HDAC2 in HEK293T cells with ectopic overexpression of TRPS1 and its truncation mutants. h Co-IP analysis of the interaction between the GATA domain of TRPS1 and USP4 and HDAC2 in HEK293T cells with ectopic overexpression of TRPS1 GATA domain truncation mutant. i MCF7 cell lysates were subjected to immunoprecipitation with control IgG or anti-TRPS1 antibody. The immunoprecipitates bound to agarose beads were eluted by elution buffer and sequential immunoprecipitation was performed with the indicated antibodies. j MCF7 and k T47D show reduced interaction between USP4 and HDAC2 upon silencing TRPS1 in Co-IP assay using anti-HDAC2 antibody. l Overexpression of USP4 decreased HDAC2 ubiquitination level and additional overexpression of TRPS1 enhanced reduction of HDAC2 ubiquitination level in HEK293T cells

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