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hdac5 overexpression lentivirus  (Genechem)

 
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    Genechem hdac5 overexpression lentivirus
    KAT2B acetylated <t>HDAC5</t> at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).
    Hdac5 Overexpression Lentivirus, supplied by Genechem, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hdac5+overexpression+lentivirus/pmc13131402-76-3-22?v=Genechem
    Average 86 stars, based on 1 article reviews
    hdac5 overexpression lentivirus - by Bioz Stars, 2026-07
    86/100 stars

    Images

    1) Product Images from "Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma"

    Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

    Journal: Journal of Advanced Research

    doi: 10.1016/j.jare.2025.08.007

    KAT2B acetylated HDAC5 at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).
    Figure Legend Snippet: KAT2B acetylated HDAC5 at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).

    Techniques Used: Binding Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Western Blot, Expressing, Over Expression, Comparison, Mutagenesis, Plasmid Preparation, Purification, Incubation, Fluorescence

    KAT2B destroyed HDAC5/LSD1 complex assembly and suppressed FASN transcriptional activity Co-IP assays were performed to verify the interaction strength between wild-type HDAC5 or the K726R mutant and Exportin1 with KAT2B overexpression. (B) Representative immunofluorescence images of wild-type HDAC5, K726R mutant HDAC5, and NES-deleted HDAC5 with KAT2B overexpression in RCC cells. (C-D) Western blots were used to assess HDAC5 and LSD1 expression in RCC cells with KAT2B overexpression or knockdown. (E) The interaction between HDAC5 and LSD1 was determined by Co-IP assays in RCC cells. (F) The interactions between HDAC5 (wild, K726Q, and K726R) and LSD1 were determined by Co-IP assays in 293 T cells. (G) RCC cells were treated with Eltanexor (60 nM) to inhibit Exportin1 activity. The levels of nuclear HDAC5, total HDAC5, Exportin1, and LSD1 were detected using Western blot. (H) Protein stability experiment of LSD1 in RCC cells with KAT2B overexpression after treated with 100 μM cycloheximide (CHX) for 0 h, 1 h, 2 h, 3 h, and 4 h and statistical diagram. (I) Following the addition of chloroquine (10 μM) or MG132 (8 μM) to RCC, LSD1 protein expression was assessed. (J) RCC cells with KAT2B overexpression were immunoprecipitated with LSD1 antibody, and the level of ubiquitin was detected. (K) LSD1 and FASN expression were detected in RCC cells with KAT2B (wild or dead) and/or HDAC5 (wild, 726Q or 726R) overexpression. (L) Schematic diagram illustrating KAT2B-mediated acetylation of HDAC5, promoting its cytoplasmic mislocalization, which resulted in the disruption of the HDAC5-LSD1 complex in the nucleus and subsequent LSD1 degradation.
    Figure Legend Snippet: KAT2B destroyed HDAC5/LSD1 complex assembly and suppressed FASN transcriptional activity Co-IP assays were performed to verify the interaction strength between wild-type HDAC5 or the K726R mutant and Exportin1 with KAT2B overexpression. (B) Representative immunofluorescence images of wild-type HDAC5, K726R mutant HDAC5, and NES-deleted HDAC5 with KAT2B overexpression in RCC cells. (C-D) Western blots were used to assess HDAC5 and LSD1 expression in RCC cells with KAT2B overexpression or knockdown. (E) The interaction between HDAC5 and LSD1 was determined by Co-IP assays in RCC cells. (F) The interactions between HDAC5 (wild, K726Q, and K726R) and LSD1 were determined by Co-IP assays in 293 T cells. (G) RCC cells were treated with Eltanexor (60 nM) to inhibit Exportin1 activity. The levels of nuclear HDAC5, total HDAC5, Exportin1, and LSD1 were detected using Western blot. (H) Protein stability experiment of LSD1 in RCC cells with KAT2B overexpression after treated with 100 μM cycloheximide (CHX) for 0 h, 1 h, 2 h, 3 h, and 4 h and statistical diagram. (I) Following the addition of chloroquine (10 μM) or MG132 (8 μM) to RCC, LSD1 protein expression was assessed. (J) RCC cells with KAT2B overexpression were immunoprecipitated with LSD1 antibody, and the level of ubiquitin was detected. (K) LSD1 and FASN expression were detected in RCC cells with KAT2B (wild or dead) and/or HDAC5 (wild, 726Q or 726R) overexpression. (L) Schematic diagram illustrating KAT2B-mediated acetylation of HDAC5, promoting its cytoplasmic mislocalization, which resulted in the disruption of the HDAC5-LSD1 complex in the nucleus and subsequent LSD1 degradation.

    Techniques Used: Activity Assay, Co-Immunoprecipitation Assay, Mutagenesis, Over Expression, Immunofluorescence, Western Blot, Expressing, Knockdown, Immunoprecipitation, Ubiquitin Proteomics, Disruption

    The KAT2B/HDAC5/LSD1/FASN axis repressed RCC lipogenesis and progression in vivo B) The picture of xenografts using Caki-1 cells with KAT2B and/or HDAC5 stable overexpressing. The tumor weight was used for statistical comparison (n = 5). (C) The tumor volume of each group was measured every six days (n = 5). (D) Representative of immunohistochemical (IHC) staining for KAT2B, HDAC5, LSD1, FASN and Ki67 in tumor xenografts. (E) Oil red O staining of the tumor xenografts with KAT2B and/or HDAC5 overexpression. (F) Living fluorescence images of mice in the metastasis model. (G-H) The liver photo and H&E staining of liver tissue in the metastatic model. Data were analyzed by one-way ANOVA (B,C).
    Figure Legend Snippet: The KAT2B/HDAC5/LSD1/FASN axis repressed RCC lipogenesis and progression in vivo B) The picture of xenografts using Caki-1 cells with KAT2B and/or HDAC5 stable overexpressing. The tumor weight was used for statistical comparison (n = 5). (C) The tumor volume of each group was measured every six days (n = 5). (D) Representative of immunohistochemical (IHC) staining for KAT2B, HDAC5, LSD1, FASN and Ki67 in tumor xenografts. (E) Oil red O staining of the tumor xenografts with KAT2B and/or HDAC5 overexpression. (F) Living fluorescence images of mice in the metastasis model. (G-H) The liver photo and H&E staining of liver tissue in the metastatic model. Data were analyzed by one-way ANOVA (B,C).

    Techniques Used: In Vivo, Comparison, Immunohistochemical staining, Immunohistochemistry, Staining, Over Expression, Fluorescence

    Graphic abstract of this research TET1-mediated promoter hypermethylation in RCC leaded to decreased KAT2B expression. Mechanistically, KAT2B acetylated HDAC5 at the K726 site and promoted its nucleus export, thereby failing to form a complex with LSD1 in nucleus. This leaded to increased histone methylation levels and decreased FASN expression, ultimately inhibiting lipogenesis and RCC progression. FASN inhibition might be useful in treating KAT2B-low RCC progression by targeting de novo lipogenesis.
    Figure Legend Snippet: Graphic abstract of this research TET1-mediated promoter hypermethylation in RCC leaded to decreased KAT2B expression. Mechanistically, KAT2B acetylated HDAC5 at the K726 site and promoted its nucleus export, thereby failing to form a complex with LSD1 in nucleus. This leaded to increased histone methylation levels and decreased FASN expression, ultimately inhibiting lipogenesis and RCC progression. FASN inhibition might be useful in treating KAT2B-low RCC progression by targeting de novo lipogenesis.

    Techniques Used: Expressing, Methylation, Inhibition



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    hdac5 overexpression lentivirus  (Genechem)
    86
    Genechem hdac5 overexpression lentivirus
    KAT2B acetylated <t>HDAC5</t> at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).
    Hdac5 Overexpression Lentivirus, supplied by Genechem, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hdac5+overexpression+lentivirus/pmc13131402-76-3-22?v=Genechem
    Average 86 stars, based on 1 article reviews
    hdac5 overexpression lentivirus - by Bioz Stars, 2026-07
    86/100 stars
    		  Buy from Supplier

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    KAT2B acetylated HDAC5 at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).

    Journal: Journal of Advanced Research

    Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

    doi: 10.1016/j.jare.2025.08.007

    Figure Lengend Snippet: KAT2B acetylated HDAC5 at K726 B) Venn diagram identifying proteins that interact with KAT2B and potentially regulate lipid metabolism (A). Among the four candidates, HDAC5 has the highest binding affinity with KAT2B (B). (C) Endogenous Co-Immunoprecipitation (Co-IP) experiments identified the interaction between KAT2B and HDAC5 in RCC cells. (D) The exogenous interaction between KAT2B and HDAC5 was determined by Co-IP assays using Flag and Myc antibodies in 293 T cells. (E) Schematic representation of full-length and truncated mutants of the KAT2B-FLAG structure. (F) FLAG-tagged full-length or truncated mutants of KAT2B were expressed in 293 T cells. Extracts were immunoprecipitated with anti-Flag or anti-HDAC5 antibodies, and bound HDAC5 or Flag was examined by western blots using anti-HDAC5 or anti-Flag antibodies. (G) Western blots were used to assess HDAC5 expression and its acetylation levels in RCC cells with KAT2B overexpression. (H) Mass spectra of the K726 site acetylation of HDAC5 after overexpression of KAT2B in 293 T cells. (I) Comparison of K726 and its surrounding residues between different species. (J) Following the overexpression of KAT2B and either wild-type HDAC5 or a K726 site mutant plasmid, the acetylation levels of HDAC5 were assessed. (K) Purified wild-type and acetyltransferase-inactive mutant KAT2B proteins were co-incubated with purified wild-type HDAC5 and K726R mutant proteins in a buffer containing acetyl-CoA. The acetylation level of HDAC5 was analyzed by western blot. (L) Representative fluorescence image of HDAC5 in RCC cells with KAT2B (wild or dead) overexpression and statistical diagram of nuclear and cytoplasmic distribution. (M) The ratio of HDAC5 nuclear fluorescence intensity to cytoplasmic fluorescence intensity in RCC with KAT2B or KAT2B dead overexpression (n = 10). (N) Nuclear HDAC5 expression in RCC cells with KAT2B (wild or dead) overexpression was assessed using western blot. Data were analyzed byone-way ANOVA (M).

    Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

    Techniques: Binding Assay, Immunoprecipitation, Co-Immunoprecipitation Assay, Western Blot, Expressing, Over Expression, Comparison, Mutagenesis, Plasmid Preparation, Purification, Incubation, Fluorescence

    KAT2B destroyed HDAC5/LSD1 complex assembly and suppressed FASN transcriptional activity Co-IP assays were performed to verify the interaction strength between wild-type HDAC5 or the K726R mutant and Exportin1 with KAT2B overexpression. (B) Representative immunofluorescence images of wild-type HDAC5, K726R mutant HDAC5, and NES-deleted HDAC5 with KAT2B overexpression in RCC cells. (C-D) Western blots were used to assess HDAC5 and LSD1 expression in RCC cells with KAT2B overexpression or knockdown. (E) The interaction between HDAC5 and LSD1 was determined by Co-IP assays in RCC cells. (F) The interactions between HDAC5 (wild, K726Q, and K726R) and LSD1 were determined by Co-IP assays in 293 T cells. (G) RCC cells were treated with Eltanexor (60 nM) to inhibit Exportin1 activity. The levels of nuclear HDAC5, total HDAC5, Exportin1, and LSD1 were detected using Western blot. (H) Protein stability experiment of LSD1 in RCC cells with KAT2B overexpression after treated with 100 μM cycloheximide (CHX) for 0 h, 1 h, 2 h, 3 h, and 4 h and statistical diagram. (I) Following the addition of chloroquine (10 μM) or MG132 (8 μM) to RCC, LSD1 protein expression was assessed. (J) RCC cells with KAT2B overexpression were immunoprecipitated with LSD1 antibody, and the level of ubiquitin was detected. (K) LSD1 and FASN expression were detected in RCC cells with KAT2B (wild or dead) and/or HDAC5 (wild, 726Q or 726R) overexpression. (L) Schematic diagram illustrating KAT2B-mediated acetylation of HDAC5, promoting its cytoplasmic mislocalization, which resulted in the disruption of the HDAC5-LSD1 complex in the nucleus and subsequent LSD1 degradation.

    Journal: Journal of Advanced Research

    Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

    doi: 10.1016/j.jare.2025.08.007

    Figure Lengend Snippet: KAT2B destroyed HDAC5/LSD1 complex assembly and suppressed FASN transcriptional activity Co-IP assays were performed to verify the interaction strength between wild-type HDAC5 or the K726R mutant and Exportin1 with KAT2B overexpression. (B) Representative immunofluorescence images of wild-type HDAC5, K726R mutant HDAC5, and NES-deleted HDAC5 with KAT2B overexpression in RCC cells. (C-D) Western blots were used to assess HDAC5 and LSD1 expression in RCC cells with KAT2B overexpression or knockdown. (E) The interaction between HDAC5 and LSD1 was determined by Co-IP assays in RCC cells. (F) The interactions between HDAC5 (wild, K726Q, and K726R) and LSD1 were determined by Co-IP assays in 293 T cells. (G) RCC cells were treated with Eltanexor (60 nM) to inhibit Exportin1 activity. The levels of nuclear HDAC5, total HDAC5, Exportin1, and LSD1 were detected using Western blot. (H) Protein stability experiment of LSD1 in RCC cells with KAT2B overexpression after treated with 100 μM cycloheximide (CHX) for 0 h, 1 h, 2 h, 3 h, and 4 h and statistical diagram. (I) Following the addition of chloroquine (10 μM) or MG132 (8 μM) to RCC, LSD1 protein expression was assessed. (J) RCC cells with KAT2B overexpression were immunoprecipitated with LSD1 antibody, and the level of ubiquitin was detected. (K) LSD1 and FASN expression were detected in RCC cells with KAT2B (wild or dead) and/or HDAC5 (wild, 726Q or 726R) overexpression. (L) Schematic diagram illustrating KAT2B-mediated acetylation of HDAC5, promoting its cytoplasmic mislocalization, which resulted in the disruption of the HDAC5-LSD1 complex in the nucleus and subsequent LSD1 degradation.

    Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

    Techniques: Activity Assay, Co-Immunoprecipitation Assay, Mutagenesis, Over Expression, Immunofluorescence, Western Blot, Expressing, Knockdown, Immunoprecipitation, Ubiquitin Proteomics, Disruption

    The KAT2B/HDAC5/LSD1/FASN axis repressed RCC lipogenesis and progression in vivo B) The picture of xenografts using Caki-1 cells with KAT2B and/or HDAC5 stable overexpressing. The tumor weight was used for statistical comparison (n = 5). (C) The tumor volume of each group was measured every six days (n = 5). (D) Representative of immunohistochemical (IHC) staining for KAT2B, HDAC5, LSD1, FASN and Ki67 in tumor xenografts. (E) Oil red O staining of the tumor xenografts with KAT2B and/or HDAC5 overexpression. (F) Living fluorescence images of mice in the metastasis model. (G-H) The liver photo and H&E staining of liver tissue in the metastatic model. Data were analyzed by one-way ANOVA (B,C).

    Journal: Journal of Advanced Research

    Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

    doi: 10.1016/j.jare.2025.08.007

    Figure Lengend Snippet: The KAT2B/HDAC5/LSD1/FASN axis repressed RCC lipogenesis and progression in vivo B) The picture of xenografts using Caki-1 cells with KAT2B and/or HDAC5 stable overexpressing. The tumor weight was used for statistical comparison (n = 5). (C) The tumor volume of each group was measured every six days (n = 5). (D) Representative of immunohistochemical (IHC) staining for KAT2B, HDAC5, LSD1, FASN and Ki67 in tumor xenografts. (E) Oil red O staining of the tumor xenografts with KAT2B and/or HDAC5 overexpression. (F) Living fluorescence images of mice in the metastasis model. (G-H) The liver photo and H&E staining of liver tissue in the metastatic model. Data were analyzed by one-way ANOVA (B,C).

    Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

    Techniques: In Vivo, Comparison, Immunohistochemical staining, Immunohistochemistry, Staining, Over Expression, Fluorescence

    Graphic abstract of this research TET1-mediated promoter hypermethylation in RCC leaded to decreased KAT2B expression. Mechanistically, KAT2B acetylated HDAC5 at the K726 site and promoted its nucleus export, thereby failing to form a complex with LSD1 in nucleus. This leaded to increased histone methylation levels and decreased FASN expression, ultimately inhibiting lipogenesis and RCC progression. FASN inhibition might be useful in treating KAT2B-low RCC progression by targeting de novo lipogenesis.

    Journal: Journal of Advanced Research

    Article Title: Epigenetically silenced KAT2B suppresses de novo lipogenesis through destroying HDAC5/LSD1 complex assembly in renal cell carcinoma

    doi: 10.1016/j.jare.2025.08.007

    Figure Lengend Snippet: Graphic abstract of this research TET1-mediated promoter hypermethylation in RCC leaded to decreased KAT2B expression. Mechanistically, KAT2B acetylated HDAC5 at the K726 site and promoted its nucleus export, thereby failing to form a complex with LSD1 in nucleus. This leaded to increased histone methylation levels and decreased FASN expression, ultimately inhibiting lipogenesis and RCC progression. FASN inhibition might be useful in treating KAT2B-low RCC progression by targeting de novo lipogenesis.

    Article Snippet: KAT2B overexpression and HDAC5 overexpression lentivirus, KAT2B‐targeted shRNA lentivirus, and overexpression plasmids of LSD1 and KAT2B (wild and enzyme-inactivated) was provided by Genechem Co. Ltd (China).

    Techniques: Expressing, Methylation, Inhibition