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https://doi.org/10.1371/journal.pone.0133448
Title: | SIRT1 interacts with and deacetylates ATP6V1B2 in mature adipocytes | Authors: | Kim S.-Y. Zhang Q. Brunmeir R. Han W. Xu F. |
Keywords: | protein ATP6V1B2 proton transporting adenosine triphosphate synthase sirtuin 1 unclassified drug ATP6V1B2 protein, mouse protein binding proton transporting adenosine triphosphate synthase sirtuin 1 3T3 cell line adipocyte Article cell maturation controlled study deacetylation embryo human human cell immunoprecipitation in vitro study in vivo study process optimization protein acetylation protein protein interaction protein targeting proteomics acetylation adipocyte animal cell differentiation cytology HEK293 cell line metabolism mouse 3T3-L1 Cells Acetylation Adipocytes Animals Cell Differentiation HEK293 Cells Humans Mice Protein Binding Proteomics Sirtuin 1 Vacuolar Proton-Translocating ATPases |
Issue Date: | 2015 | Citation: | Kim S.-Y., Zhang Q., Brunmeir R., Han W., Xu F. (2015). SIRT1 interacts with and deacetylates ATP6V1B2 in mature adipocytes. PLoS ONE 10 (7) : e0133448. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0133448 | Rights: | Attribution 4.0 International | Abstract: | SIRT1 plays a key role in maintaining metabolic homeostasis in mammals by directly modulating the activities of various transcription factors and metabolic enzymes through lysine deacetylation. White adipose tissue plays a key role in lipid storage and metabolism. To identify novel molecular targets of SIRT1 in fat cells, we used a non-biased proteomic approach.We identified a number of proteins whose acetylation status was significantly affected by SIRT1 modulator treatment in 3T3-L1 adipocytes. Among them, ATP6V1B2, a subunit of the vacuolar (H+)-ATPase, was further shown to be associated with SIRT1 by coimmunoprecipitation assay. Moreover, SIRT1 deacetylates ATP6V1B2 in vitro and in vivo. Taken together, our study demonstrates that ATP6V1B2 is a molecular target of SIRT1 in fat cells and the role of SIRT1 and ATP6V1B2 acetylation in the vacuolar (H+)-ATPase function warrants further investigation. Copyright: © 2015 Kim et al. | Source Title: | PLoS ONE | URI: | https://scholarbank.nus.edu.sg/handle/10635/161498 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0133448 | Rights: | Attribution 4.0 International |
Appears in Collections: | Staff Publications Elements |
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