| http://purl.uniprot.org/citations/28065600 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28065600 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28065600 | http://www.w3.org/2000/01/rdf-schema#comment | "In mammalian cells, histone deacetylase (HDAC) and Sirtuin (SIRT) are two families responsible for removing acetyl groups from acetylated proteins. Here, we describe protein deacetylation coupled with deacetylimination as a function of lysyl oxidase (LOX) family members. LOX-like 3 (Loxl3) associates with Stat3 in the nucleus to deacetylate and deacetyliminate Stat3 on multiple acetyl-lysine sites. Surprisingly, Loxl3 N-terminal scavenger receptor cysteine-rich (SRCR) repeats, rather than the C-terminal oxidase catalytic domain, represent the major deacetylase/deacetyliminase activity. Loxl3-mediated deacetylation/deacetylimination disrupts Stat3 dimerization, abolishes Stat3 transcription activity, and restricts cell proliferation. In Loxl3-/-mice, Stat3 is constitutively acetylated and naive CD4+ T cells are potentiated in Th17/Treg cell differentiation. When overexpressed, the SRCR repeats from other LOX family members can catalyze protein deacetylation/deacetylimination. Thus, our findings delineate a hitherto-unknown mechanism of protein deacetylation and deacetylimination catalyzed by lysyl oxidases."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2016.12.002"xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2016.12.002"xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Cheng J."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Cheng J."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Ma L."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Ma L."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Huang C."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Huang C."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Wang C."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Wang C."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Zhang X."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Zhang X."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Wang Y.M."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Wang Y.M."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Zhang Y.S."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Zhang Y.S."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Yang J.H."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Yang J.H."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Chang Z."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Chang Z."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Chatterjee D."xsd:string |
| http://purl.uniprot.org/citations/28065600 | http://purl.uniprot.org/core/author | "Chatterjee D."xsd:string |