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Title:
PPARα regulates YAP protein levels and activity by affecting its ubiquitination modification | BMC Biology | Full Text
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Background Peroxisome proliferator-activated receptor α (PPARα) plays a crucial role in liver physiological and pathological processes. Yes-associated protein (YAP) is a key effector in regulating cell growth and organ size. Ubiquitination is known to modulate YAP protein expression, stability, and nuclear localization. Our previous study demonstrated that PPARα activation promotes hepatomegaly and liver regeneration via YAP activation. However, the underlying molecular mechanisms by which PPARα regulates YAP are unclear. In this study, PPARα was activated by the classical agonist WY-14643, and its effects on YAP ubiquitination were examined using plasmid transfection and immunoprecipitation. The ubiquitination of YAP was further investigated through mutant YAP plasmids, gene knockdown, and immunofluorescence staining. YAP mRNA and protein expression were measured via qRT-PCR and western blotting. Results The results demonstrated that PPARα activation upregulated YAP protein levels and enhanced its activity, while reducing overall YAP ubiquitination. Specifically, PPARα activation inhibited K48-linked ubiquitination while promoting K63-linked ubiquitination of YAP. Mutations at the K252, K321, and K497 residues of YAP markedly reduced the capacity of PPARα activation to facilitate YAP nuclear translocation. Furthermore, knockdown of the E3 ligase TRAF6 abolished the PPARα-induced K63-linked ubiquitination of YAP and the upregulation of its downstream target genes. Conclusions These findings highlight the pivotal role of ubiquitination in regulating YAP through PPARα activation, providing novel insights for future studies on the post-translational regulation of YAP by PPARα activation.
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headline:PPARα regulates YAP protein levels and activity by affecting its ubiquitination modification
description:Peroxisome proliferator-activated receptor α (PPARα) plays a crucial role in liver physiological and pathological processes. Yes-associated protein (YAP) is a key effector in regulating cell growth and organ size. Ubiquitination is known to modulate YAP protein expression, stability, and nuclear localization. Our previous study demonstrated that PPARα activation promotes hepatomegaly and liver regeneration via YAP activation. However, the underlying molecular mechanisms by which PPARα regulates YAP are unclear. In this study, PPARα was activated by the classical agonist WY-14643, and its effects on YAP ubiquitination were examined using plasmid transfection and immunoprecipitation. The ubiquitination of YAP was further investigated through mutant YAP plasmids, gene knockdown, and immunofluorescence staining. YAP mRNA and protein expression were measured via qRT-PCR and western blotting. The results demonstrated that PPARα activation upregulated YAP protein levels and enhanced its activity, while reducing overall YAP ubiquitination. Specifically, PPARα activation inhibited K48-linked ubiquitination while promoting K63-linked ubiquitination of YAP. Mutations at the K252, K321, and K497 residues of YAP markedly reduced the capacity of PPARα activation to facilitate YAP nuclear translocation. Furthermore, knockdown of the E3 ligase TRAF6 abolished the PPARα-induced K63-linked ubiquitination of YAP and the upregulation of its downstream target genes. These findings highlight the pivotal role of ubiquitination in regulating YAP through PPARα activation, providing novel insights for future studies on the post-translational regulation of YAP by PPARα activation.
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Peroxisome proliferator-activated receptor α
Yes-associated protein
Ubiquitination
TRAF6
Life Sciences
general
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headline:PPARα regulates YAP protein levels and activity by affecting its ubiquitination modification
description:Peroxisome proliferator-activated receptor α (PPARα) plays a crucial role in liver physiological and pathological processes. Yes-associated protein (YAP) is a key effector in regulating cell growth and organ size. Ubiquitination is known to modulate YAP protein expression, stability, and nuclear localization. Our previous study demonstrated that PPARα activation promotes hepatomegaly and liver regeneration via YAP activation. However, the underlying molecular mechanisms by which PPARα regulates YAP are unclear. In this study, PPARα was activated by the classical agonist WY-14643, and its effects on YAP ubiquitination were examined using plasmid transfection and immunoprecipitation. The ubiquitination of YAP was further investigated through mutant YAP plasmids, gene knockdown, and immunofluorescence staining. YAP mRNA and protein expression were measured via qRT-PCR and western blotting. The results demonstrated that PPARα activation upregulated YAP protein levels and enhanced its activity, while reducing overall YAP ubiquitination. Specifically, PPARα activation inhibited K48-linked ubiquitination while promoting K63-linked ubiquitination of YAP. Mutations at the K252, K321, and K497 residues of YAP markedly reduced the capacity of PPARα activation to facilitate YAP nuclear translocation. Furthermore, knockdown of the E3 ligase TRAF6 abolished the PPARα-induced K63-linked ubiquitination of YAP and the upregulation of its downstream target genes. These findings highlight the pivotal role of ubiquitination in regulating YAP through PPARα activation, providing novel insights for future studies on the post-translational regulation of YAP by PPARα activation.
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Yes-associated protein
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TRAF6
Life Sciences
general
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name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
type:PostalAddress
type:Organization
email:[email protected]
name:Huichang Bi
affiliation:
name:Southern Medical University
address:
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
type:PostalAddress
type:Organization
name:Shenzhen Graduate School of Peking University
address:
name:The State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School of Peking University, Shenzhen, China
type:PostalAddress
type:Organization
email:[email protected]
PostalAddress:
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:Department of Pharmacy, The Sixth Affiliated Hospital, School of Medicine, South China University of Technology, Foshan, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:The State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School of Peking University, Shenzhen, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:Department of Pharmacy, The Sixth Affiliated Hospital, School of Medicine, South China University of Technology, Foshan, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:NMPA Key Laboratory for Research and Evaluation of Drug Metabolism & Guangdong Provincial Key Laboratory of New Drug Screening & Guangdong-Hongkong-Macao Joint Laboratory for New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, China
name:The State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School of Peking University, Shenzhen, China
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