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10.1007/s13238-016-0324-z http://scihub22266oqcxt.onion/10.1007/s13238-016-0324-z C5326618!5326618 !27743347     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27743347 &cmd=llinks): Failed to open stream: HTTP request failed! 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E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain |pdf=|usr=}}{{27743347 }} gab.com Text E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain JO: Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=27743347 #FOAvip UHRF2 is a ubiquitin-protein ligase E3 that regulates cell cycle, genomic stability and epigenetics. We conducted a co-immunoprecipitation assay and found that TIP60 and HDAC1 interact with UHRF2. We previously demonstrated that UHRF2 regulated H3K9ac and H3K14ac differentially in normal and cancer cells. However, the accurate signal transduction mechanisms were not clear. In this study, we found that TIP60 acted downstream of UHRF2 to regulate H3K9ac and H3K14ac expression. TIP60 is stabilized in normal cells by UHRF2 ubiquitination. However, TIP60 is destabilized in cancer cells. Depletion or inhibition of TIP60 disrupts the regulatory relationship between UHRF2, H3K9ac and H3K14ac. In summary, the findings suggest that UHRF2 mediated the post-translational modification of histones and the initiation and progression of cancer. Twit Text FOAVip E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain ????Protein Cell http://www.kidney.de/pget.php?&tw=1&pmid=27743347 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27743347 #FOAvip English Wikipedia <ref>{{Cite pmid|27743347 }}</ref> E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H3K9ac and H3K14ac via RING finger domain #MMPMID27743347 Zeng S ; Wang Y ; Zhang T ; Bai L ; Wang Y ; Duan C Protein Cell 2017[Mar]; 8 (3 ): 202-218 PMID27743347 show ga UHRF2 is a ubiquitin-protein ligase E3 that regulates cell cycle, genomic stability and epigenetics. We conducted a co-immunoprecipitation assay and found that TIP60 and HDAC1 interact with UHRF2. We previously demonstrated that UHRF2 regulated H3K9ac and H3K14ac differentially in normal and cancer cells. However, the accurate signal transduction mechanisms were not clear. In this study, we found that TIP60 acted downstream of UHRF2 to regulate H3K9ac and H3K14ac expression. TIP60 is stabilized in normal cells by UHRF2 ubiquitination. However, TIP60 is destabilized in cancer cells. Depletion or inhibition of TIP60 disrupts the regulatory relationship between UHRF2, H3K9ac and H3K14ac. In summary, the findings suggest that UHRF2 mediated the post-translational modification of histones and the initiation and progression of cancer. |*Ubiquitination [MESH] |Cell Line [MESH] |Histone Acetyltransferases/genetics/*metabolism [MESH] |Histones/genetics/*metabolism [MESH] |Humans [MESH] |Lysine Acetyltransferase 5 [MESH] |Neoplasm Proteins/genetics/*metabolism [MESH] |Neoplasms/genetics/*metabolism [MESH] |RING Finger Domains [MESH]E3 ligase UHRF2 stabilizes the acetyltransferase TIP60 and regulates H(epmc).pdf DeepDyve Pubget Overpricing