WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112
WIP1, as a critical phosphatase, plays many important roles in various physiological and pathological processes through dephosphorylating different substrate proteins. However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show imp...
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| Veröffentlicht in: | Cellular and molecular life sciences : CMLS 2017-06, Vol.74 (11), p.2067-2079 |
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| container_title | Cellular and molecular life sciences : CMLS |
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| creator | Li, Dahu Zhang, Lijun Xu, Lun Liu, Lili He, Yunling Zhang, Yiyao Huang, Xin Zhao, Tong Wu, Liying Zhao, Yongqi Wu, Kuiwu Li, Hui Yu, Xiao Zhao, Taiyun Gong, Shenghui Fan, Ming Zhu, Lingling |
| description | WIP1, as a critical phosphatase, plays many important roles in various physiological and pathological processes through dephosphorylating different substrate proteins. However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show impaired body weight growth, dramatically decreased fat mass, and significantly reduced triglyceride and leptin levels in circulation. This dysregulation of adipose development caused by the deletion of WIP1 occurs as early as adipogenesis. In contrast, lentivirus-mediated WIP1 phosphatase overexpression significantly increases the adipogenesis of pre-adipocytes via an enzymatic activity-dependent mechanism. PPARγ is a master gene of adipogenesis, and the phosphorylation of PPARγ at serine 112 strongly inhibits adipogenesis; however, very little is known about the negative regulation of this phosphorylation. Here, we show that WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARγ and dephosphorylating p-PPARγ S112 in vitro and in vivo. |
| doi_str_mv | 10.1007/s00018-016-2450-4 |
| format | Article |
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However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show impaired body weight growth, dramatically decreased fat mass, and significantly reduced triglyceride and leptin levels in circulation. This dysregulation of adipose development caused by the deletion of WIP1 occurs as early as adipogenesis. In contrast, lentivirus-mediated WIP1 phosphatase overexpression significantly increases the adipogenesis of pre-adipocytes via an enzymatic activity-dependent mechanism. PPARγ is a master gene of adipogenesis, and the phosphorylation of PPARγ at serine 112 strongly inhibits adipogenesis; however, very little is known about the negative regulation of this phosphorylation. Here, we show that WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARγ and dephosphorylating p-PPARγ S112 in vitro and in vivo.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-016-2450-4</identifier><identifier>PMID: 28180926</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Adipocytes - cytology ; Adipocytes - metabolism ; Adipogenesis ; Adiposity ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Body Weight ; Cell Biology ; Cell Line ; Cell Size ; Gene Expression Regulation ; Gene Knockdown Techniques ; Humans ; Leptin - blood ; Life Sciences ; Mice, Inbred C57BL ; Mice, Knockout ; Original ; Original Article ; Phosphorylation ; Phosphoserine - metabolism ; PPAR gamma - metabolism ; Protein Binding ; Protein Phosphatase 2C - deficiency ; Protein Phosphatase 2C - metabolism ; Triglycerides - blood</subject><ispartof>Cellular and molecular life sciences : CMLS, 2017-06, Vol.74 (11), p.2067-2079</ispartof><rights>Springer International Publishing 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c400t-2f8b57ed03e67f67540a62637c1a2d2b0a9c796634d4772caa0c58b56b7544dd3</citedby><cites>FETCH-LOGICAL-c400t-2f8b57ed03e67f67540a62637c1a2d2b0a9c796634d4772caa0c58b56b7544dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11107755/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11107755/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41464,42533,51294,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28180926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Dahu</creatorcontrib><creatorcontrib>Zhang, Lijun</creatorcontrib><creatorcontrib>Xu, Lun</creatorcontrib><creatorcontrib>Liu, Lili</creatorcontrib><creatorcontrib>He, Yunling</creatorcontrib><creatorcontrib>Zhang, Yiyao</creatorcontrib><creatorcontrib>Huang, Xin</creatorcontrib><creatorcontrib>Zhao, Tong</creatorcontrib><creatorcontrib>Wu, Liying</creatorcontrib><creatorcontrib>Zhao, Yongqi</creatorcontrib><creatorcontrib>Wu, Kuiwu</creatorcontrib><creatorcontrib>Li, Hui</creatorcontrib><creatorcontrib>Yu, Xiao</creatorcontrib><creatorcontrib>Zhao, Taiyun</creatorcontrib><creatorcontrib>Gong, Shenghui</creatorcontrib><creatorcontrib>Fan, Ming</creatorcontrib><creatorcontrib>Zhu, Lingling</creatorcontrib><title>WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112</title><title>Cellular and molecular life sciences : CMLS</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>WIP1, as a critical phosphatase, plays many important roles in various physiological and pathological processes through dephosphorylating different substrate proteins. However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show impaired body weight growth, dramatically decreased fat mass, and significantly reduced triglyceride and leptin levels in circulation. This dysregulation of adipose development caused by the deletion of WIP1 occurs as early as adipogenesis. In contrast, lentivirus-mediated WIP1 phosphatase overexpression significantly increases the adipogenesis of pre-adipocytes via an enzymatic activity-dependent mechanism. PPARγ is a master gene of adipogenesis, and the phosphorylation of PPARγ at serine 112 strongly inhibits adipogenesis; however, very little is known about the negative regulation of this phosphorylation. Here, we show that WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARγ and dephosphorylating p-PPARγ S112 in vitro and in vivo.</description><subject>Adipocytes - cytology</subject><subject>Adipocytes - metabolism</subject><subject>Adipogenesis</subject><subject>Adiposity</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Body Weight</subject><subject>Cell Biology</subject><subject>Cell Line</subject><subject>Cell Size</subject><subject>Gene Expression Regulation</subject><subject>Gene Knockdown Techniques</subject><subject>Humans</subject><subject>Leptin - blood</subject><subject>Life Sciences</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Original</subject><subject>Original Article</subject><subject>Phosphorylation</subject><subject>Phosphoserine - metabolism</subject><subject>PPAR gamma - metabolism</subject><subject>Protein Binding</subject><subject>Protein Phosphatase 2C - deficiency</subject><subject>Protein Phosphatase 2C - metabolism</subject><subject>Triglycerides - blood</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kNtKxDAQhoMonh_AG8kLVCfZNGmvRMTDwoKLKHoXsknaRmpTkq6wz-V7-ExmqS5649UMzPf_Ax9CJwTOCIA4jwBAigwIzyjLIWNbaJ8wClkJgmx_77ygL3voIMbXBOcF5btojxakgJLyfWSep3OC-8bHvlGDiha7iBXWwQ1OqxYHWy9bNfiAfYWVcb2vbWdjgoYm-GXdYGPHtA-rBLquxvP55cPnB442uM5iQugR2qlUG-3x9zxETzfXj1d32ez-dnp1Ocs0AxgyWhWLXFgDE8tFxUXOQHHKJ0ITRQ1dgCq1KDmfMMOEoFop0HmK8EVCmTGTQ3Qx9vbLxZs12nZDUK3sg3tTYSW9cvLvpXONrP27JISAEHmeGsjYoIOPMdhqEyYg187l6Fwm53LtXLKUOf39dZP4kZwAOgIxnbraBvnql6FLJv5p_QLFQI7B</recordid><startdate>20170601</startdate><enddate>20170601</enddate><creator>Li, Dahu</creator><creator>Zhang, Lijun</creator><creator>Xu, Lun</creator><creator>Liu, Lili</creator><creator>He, Yunling</creator><creator>Zhang, Yiyao</creator><creator>Huang, Xin</creator><creator>Zhao, Tong</creator><creator>Wu, Liying</creator><creator>Zhao, Yongqi</creator><creator>Wu, Kuiwu</creator><creator>Li, Hui</creator><creator>Yu, Xiao</creator><creator>Zhao, Taiyun</creator><creator>Gong, Shenghui</creator><creator>Fan, Ming</creator><creator>Zhu, Lingling</creator><general>Springer International Publishing</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>5PM</scope></search><sort><creationdate>20170601</creationdate><title>WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112</title><author>Li, Dahu ; Zhang, Lijun ; Xu, Lun ; Liu, Lili ; He, Yunling ; Zhang, Yiyao ; Huang, Xin ; Zhao, Tong ; Wu, Liying ; Zhao, Yongqi ; Wu, Kuiwu ; Li, Hui ; Yu, Xiao ; Zhao, Taiyun ; Gong, Shenghui ; Fan, Ming ; Zhu, Lingling</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c400t-2f8b57ed03e67f67540a62637c1a2d2b0a9c796634d4772caa0c58b56b7544dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Adipocytes - cytology</topic><topic>Adipocytes - metabolism</topic><topic>Adipogenesis</topic><topic>Adiposity</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Body Weight</topic><topic>Cell Biology</topic><topic>Cell Line</topic><topic>Cell Size</topic><topic>Gene Expression Regulation</topic><topic>Gene Knockdown Techniques</topic><topic>Humans</topic><topic>Leptin - blood</topic><topic>Life Sciences</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Original</topic><topic>Original Article</topic><topic>Phosphorylation</topic><topic>Phosphoserine - metabolism</topic><topic>PPAR gamma - metabolism</topic><topic>Protein Binding</topic><topic>Protein Phosphatase 2C - deficiency</topic><topic>Protein Phosphatase 2C - metabolism</topic><topic>Triglycerides - blood</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Dahu</creatorcontrib><creatorcontrib>Zhang, Lijun</creatorcontrib><creatorcontrib>Xu, Lun</creatorcontrib><creatorcontrib>Liu, Lili</creatorcontrib><creatorcontrib>He, Yunling</creatorcontrib><creatorcontrib>Zhang, Yiyao</creatorcontrib><creatorcontrib>Huang, Xin</creatorcontrib><creatorcontrib>Zhao, Tong</creatorcontrib><creatorcontrib>Wu, Liying</creatorcontrib><creatorcontrib>Zhao, Yongqi</creatorcontrib><creatorcontrib>Wu, Kuiwu</creatorcontrib><creatorcontrib>Li, Hui</creatorcontrib><creatorcontrib>Yu, Xiao</creatorcontrib><creatorcontrib>Zhao, Taiyun</creatorcontrib><creatorcontrib>Gong, Shenghui</creatorcontrib><creatorcontrib>Fan, Ming</creatorcontrib><creatorcontrib>Zhu, Lingling</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and molecular life sciences : CMLS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Dahu</au><au>Zhang, Lijun</au><au>Xu, Lun</au><au>Liu, Lili</au><au>He, Yunling</au><au>Zhang, Yiyao</au><au>Huang, Xin</au><au>Zhao, Tong</au><au>Wu, Liying</au><au>Zhao, Yongqi</au><au>Wu, Kuiwu</au><au>Li, Hui</au><au>Yu, Xiao</au><au>Zhao, Taiyun</au><au>Gong, Shenghui</au><au>Fan, Ming</au><au>Zhu, Lingling</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112</atitle><jtitle>Cellular and molecular life sciences : CMLS</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2017-06-01</date><risdate>2017</risdate><volume>74</volume><issue>11</issue><spage>2067</spage><epage>2079</epage><pages>2067-2079</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><abstract>WIP1, as a critical phosphatase, plays many important roles in various physiological and pathological processes through dephosphorylating different substrate proteins. However, the functions of WIP1 in adipogenesis and fat accumulation are not clear. Here, we report that WIP1-deficient mice show impaired body weight growth, dramatically decreased fat mass, and significantly reduced triglyceride and leptin levels in circulation. This dysregulation of adipose development caused by the deletion of WIP1 occurs as early as adipogenesis. In contrast, lentivirus-mediated WIP1 phosphatase overexpression significantly increases the adipogenesis of pre-adipocytes via an enzymatic activity-dependent mechanism. PPARγ is a master gene of adipogenesis, and the phosphorylation of PPARγ at serine 112 strongly inhibits adipogenesis; however, very little is known about the negative regulation of this phosphorylation. Here, we show that WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARγ and dephosphorylating p-PPARγ S112 in vitro and in vivo.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>28180926</pmid><doi>10.1007/s00018-016-2450-4</doi><tpages>13</tpages></addata></record> |
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| ispartof | Cellular and molecular life sciences : CMLS, 2017-06, Vol.74 (11), p.2067-2079 |
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| subjects | Adipocytes - cytology Adipocytes - metabolism Adipogenesis Adiposity Animals Biochemistry Biomedical and Life Sciences Biomedicine Body Weight Cell Biology Cell Line Cell Size Gene Expression Regulation Gene Knockdown Techniques Humans Leptin - blood Life Sciences Mice, Inbred C57BL Mice, Knockout Original Original Article Phosphorylation Phosphoserine - metabolism PPAR gamma - metabolism Protein Binding Protein Phosphatase 2C - deficiency Protein Phosphatase 2C - metabolism Triglycerides - blood |
| title | WIP1 phosphatase is a critical regulator of adipogenesis through dephosphorylating PPARγ serine 112 |
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