YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice

The subcellular localization of Yes-associated protein (YAP) is dynamically regulated by post-transcriptional modifications, critically influencing cardiac function. Despite its significance, the precise mechanism controlling YAP nuclear sequestration and its role in cardiac hypertrophy remain poorl...

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Main Authors: Panxia Wang, Luping Wang, Cui Liu, Yuehuai Hu, Guodong Feng, Zuqian Lian, Jing Lu, Ping He, Hexin Cai, Xiaohui Liang, Peiqing Liu, Xiaoqian Wu
Format: Article
Language:English
Published: Elsevier 2025-01-01
Series:Pharmacological Research
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Online Access:http://www.sciencedirect.com/science/article/pii/S1043661824005188
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author Panxia Wang
Luping Wang
Cui Liu
Yuehuai Hu
Guodong Feng
Zuqian Lian
Jing Lu
Ping He
Hexin Cai
Xiaohui Liang
Peiqing Liu
Xiaoqian Wu
author_facet Panxia Wang
Luping Wang
Cui Liu
Yuehuai Hu
Guodong Feng
Zuqian Lian
Jing Lu
Ping He
Hexin Cai
Xiaohui Liang
Peiqing Liu
Xiaoqian Wu
author_sort Panxia Wang
collection DOAJ
description The subcellular localization of Yes-associated protein (YAP) is dynamically regulated by post-transcriptional modifications, critically influencing cardiac function. Despite its significance, the precise mechanism controlling YAP nuclear sequestration and its role in cardiac hypertrophy remain poorly defined. In this study, utilizing immunoprecipitation-mass spectrometry, we identified potential acetylation sites and interacting proteins of YAP. Co-immunoprecipitation and immunofluorescence assays were used to elucidate the protein interactions and subcellular colocalization. We found that YAP protected against ISO-induced pathological cardiac hypertrophy both in vivo and in vitro. During cardiac hypertrophy YAP acetylation increased while its nuclear accumulation reduced without altering Ser127 phosphorylation. Notably, lysine 236 was identified as a novel acetylation site on YAP. Acetylation at K236 facilitated YAP’s nucleic export, suppressed the expression of target genes such as NRF1 and Cox IV, and counteracted YAP's anti-hypertrophic effects. Importantly, deacetylase SIRT6 was identified as a regulator of YAP deacetylation, disrupting the YAP with chaperone protein 14–3–3 interaction and inhibiting YAP’s nuclear export, thereby facilitating cardiac protective role of YAP. This study identified YAP K236 acetylation as a key regulator of its nuclear retention in cardiomyocytes, with SIRT6-mediated deacetylation facilitating YAP’s protective effects against cardiac hypertrophy. Targeting YAP acetylation may offer a promising therapeutic strategy for cardiac hypertrophy.
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spelling doaj-art-7d7669ca55cd4d51973046ae5e4be56e2025-08-20T02:44:24ZengElsevierPharmacological Research1096-11862025-01-0121110757310.1016/j.phrs.2024.107573YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in micePanxia Wang0Luping Wang1Cui Liu2Yuehuai Hu3Guodong Feng4Zuqian Lian5Jing Lu6Ping He7Hexin Cai8Xiaohui Liang9Peiqing Liu10Xiaoqian Wu11Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR ChinaGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR ChinaSchool of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, PR ChinaSchool of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, PR ChinaSchool of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, PR ChinaGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR ChinaSchool of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, PR ChinaDepartment of Pharmacy, The Eighth Affiliated Hospital, Sun Yat-sen University, Shennan Rord 3025, Shenzhen 518033, PR ChinaGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR ChinaThe First Affiliated Hospital of Guangzhou Medical University, Guangzhou 511436, PR ChinaGuangdong Provincial Key Laboratory of New Drug Design and Evaluation, Sun Yat-sen University, Guangzhou 510006, PR China; Guangdong Provincial Engineering Laboratory of Druggability and New Drugs Evaluation, Guangzhou 510006, PR China; Corresponding author at: Guangdong Provincial Key Laboratory of New Drug Design and Evaluation, Sun Yat-sen University, Guangzhou 510006, PR China.Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR China; Corresponding author.The subcellular localization of Yes-associated protein (YAP) is dynamically regulated by post-transcriptional modifications, critically influencing cardiac function. Despite its significance, the precise mechanism controlling YAP nuclear sequestration and its role in cardiac hypertrophy remain poorly defined. In this study, utilizing immunoprecipitation-mass spectrometry, we identified potential acetylation sites and interacting proteins of YAP. Co-immunoprecipitation and immunofluorescence assays were used to elucidate the protein interactions and subcellular colocalization. We found that YAP protected against ISO-induced pathological cardiac hypertrophy both in vivo and in vitro. During cardiac hypertrophy YAP acetylation increased while its nuclear accumulation reduced without altering Ser127 phosphorylation. Notably, lysine 236 was identified as a novel acetylation site on YAP. Acetylation at K236 facilitated YAP’s nucleic export, suppressed the expression of target genes such as NRF1 and Cox IV, and counteracted YAP's anti-hypertrophic effects. Importantly, deacetylase SIRT6 was identified as a regulator of YAP deacetylation, disrupting the YAP with chaperone protein 14–3–3 interaction and inhibiting YAP’s nuclear export, thereby facilitating cardiac protective role of YAP. This study identified YAP K236 acetylation as a key regulator of its nuclear retention in cardiomyocytes, with SIRT6-mediated deacetylation facilitating YAP’s protective effects against cardiac hypertrophy. Targeting YAP acetylation may offer a promising therapeutic strategy for cardiac hypertrophy.http://www.sciencedirect.com/science/article/pii/S1043661824005188Cardiac hypertrophyYAPK236 residuesAcetylationSIRT6
spellingShingle Panxia Wang
Luping Wang
Cui Liu
Yuehuai Hu
Guodong Feng
Zuqian Lian
Jing Lu
Ping He
Hexin Cai
Xiaohui Liang
Peiqing Liu
Xiaoqian Wu
YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
Pharmacological Research
Cardiac hypertrophy
YAP
K236 residues
Acetylation
SIRT6
title YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
title_full YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
title_fullStr YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
title_full_unstemmed YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
title_short YAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
title_sort yap k236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice
topic Cardiac hypertrophy
YAP
K236 residues
Acetylation
SIRT6
url http://www.sciencedirect.com/science/article/pii/S1043661824005188
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