Please use this identifier to cite or link to this item: 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
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