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Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis

BECN1, a protein essential for autophagy, is involved in adipocyte differentiation, lipolysis and insulin resistance. The discovery of new mechanisms for modifying BECN1 in adipocytes may provide novel therapeutic targets for obesity. This study aimed to investigate the impact of mutations at the ac...

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Autores principales: Li, Chengqian, Xu, Jun, Yu, Qing, Wang, Ping, Dong, Bingzi, Shen, Liyan, Wang, Qing, Li, Shufa, Yang, Ying, Deng, Yujie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8278081/
https://www.ncbi.nlm.nih.gov/pubmed/34085745
http://dx.doi.org/10.1111/jcmm.16692
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author Li, Chengqian
Xu, Jun
Yu, Qing
Wang, Ping
Dong, Bingzi
Shen, Liyan
Wang, Qing
Li, Shufa
Yang, Ying
Deng, Yujie
author_facet Li, Chengqian
Xu, Jun
Yu, Qing
Wang, Ping
Dong, Bingzi
Shen, Liyan
Wang, Qing
Li, Shufa
Yang, Ying
Deng, Yujie
author_sort Li, Chengqian
collection PubMed
description BECN1, a protein essential for autophagy, is involved in adipocyte differentiation, lipolysis and insulin resistance. The discovery of new mechanisms for modifying BECN1 in adipocytes may provide novel therapeutic targets for obesity. This study aimed to investigate the impact of mutations at the acetylation sites of BECN1 on adipocyte differentiation and lipolysis. We found that Ace‐BECN1 levels were increased in 3T3‐L1 adipocyte differentiation and isoproterenol‐/TNF‐α‐stimulated lipolysis and in subcutaneous and visceral adipose tissues of high‐fat diet mice. K414 was identified as an acetylation site of BECN1, which affects the stability of the BECN1 protein. Mutation at K414 of BECN1 affected autophagy, differentiation and lipolysis in 3T3‐L1 adipocytes. These data indicated the potential of BECN1 K414 as a key molecule and a drug target for regulating autophagy and lipid metabolism in adipocytes.
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spelling pubmed-82780812021-07-15 Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis Li, Chengqian Xu, Jun Yu, Qing Wang, Ping Dong, Bingzi Shen, Liyan Wang, Qing Li, Shufa Yang, Ying Deng, Yujie J Cell Mol Med Original Articles BECN1, a protein essential for autophagy, is involved in adipocyte differentiation, lipolysis and insulin resistance. The discovery of new mechanisms for modifying BECN1 in adipocytes may provide novel therapeutic targets for obesity. This study aimed to investigate the impact of mutations at the acetylation sites of BECN1 on adipocyte differentiation and lipolysis. We found that Ace‐BECN1 levels were increased in 3T3‐L1 adipocyte differentiation and isoproterenol‐/TNF‐α‐stimulated lipolysis and in subcutaneous and visceral adipose tissues of high‐fat diet mice. K414 was identified as an acetylation site of BECN1, which affects the stability of the BECN1 protein. Mutation at K414 of BECN1 affected autophagy, differentiation and lipolysis in 3T3‐L1 adipocytes. These data indicated the potential of BECN1 K414 as a key molecule and a drug target for regulating autophagy and lipid metabolism in adipocytes. John Wiley and Sons Inc. 2021-06-04 2021-07 /pmc/articles/PMC8278081/ /pubmed/34085745 http://dx.doi.org/10.1111/jcmm.16692 Text en © 2021 The Authors. Journal of Cellular and Molecular Medicine published by Foundation for Cellular and Molecular Medicine and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Li, Chengqian
Xu, Jun
Yu, Qing
Wang, Ping
Dong, Bingzi
Shen, Liyan
Wang, Qing
Li, Shufa
Yang, Ying
Deng, Yujie
Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title_full Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title_fullStr Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title_full_unstemmed Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title_short Mutation of the novel acetylation site at K414R of BECN1 is involved in adipocyte differentiation and lipolysis
title_sort mutation of the novel acetylation site at k414r of becn1 is involved in adipocyte differentiation and lipolysis
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8278081/
https://www.ncbi.nlm.nih.gov/pubmed/34085745
http://dx.doi.org/10.1111/jcmm.16692
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