FAM122A, a new endogenous inhibitor of protein phosphatase 2A
The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interact...
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| Veröffentlicht in: | Oncotarget 2016-09, Vol.7 (39), p.63887-63900 |
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| creator | Fan, Li Liu, Man-Hua Guo, Meng Hu, Chuan-Xi Yan, Zhao-Wen Chen, Jing Chen, Guo-Qiang Huang, Ying |
| description | The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated. |
| doi_str_mv | 10.18632/oncotarget.11698 |
| format | Article |
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In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated.</description><identifier>ISSN: 1949-2553</identifier><identifier>EISSN: 1949-2553</identifier><identifier>DOI: 10.18632/oncotarget.11698</identifier><identifier>PMID: 27588481</identifier><language>eng</language><publisher>United States: Impact Journals LLC</publisher><subject>A549 Cells ; Catalytic Domain ; Cell Line, Tumor ; Cell Proliferation ; Enzyme Inhibitors - pharmacology ; Gene Expression Regulation, Neoplastic ; Gene Silencing ; HEK293 Cells ; HeLa Cells ; Humans ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 2 - antagonists & inhibitors ; Protein Phosphatase 2 - metabolism ; Protein Phosphatase 2C - metabolism ; Protein Processing, Post-Translational ; Protein Subunits - genetics ; Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism ; Research Paper ; Ubiquitination</subject><ispartof>Oncotarget, 2016-09, Vol.7 (39), p.63887-63900</ispartof><rights>Copyright: © 2016 Fan et al. 2016</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c426t-1b2b4088345f0b7064deb2a2cf28ad76c2daedcd7dd09766f3c4eb5a2b725f7d3</citedby><cites>FETCH-LOGICAL-c426t-1b2b4088345f0b7064deb2a2cf28ad76c2daedcd7dd09766f3c4eb5a2b725f7d3</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/PMC5325411/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5325411/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27588481$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fan, Li</creatorcontrib><creatorcontrib>Liu, Man-Hua</creatorcontrib><creatorcontrib>Guo, Meng</creatorcontrib><creatorcontrib>Hu, Chuan-Xi</creatorcontrib><creatorcontrib>Yan, Zhao-Wen</creatorcontrib><creatorcontrib>Chen, Jing</creatorcontrib><creatorcontrib>Chen, Guo-Qiang</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><title>FAM122A, a new endogenous inhibitor of protein phosphatase 2A</title><title>Oncotarget</title><addtitle>Oncotarget</addtitle><description>The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated.</description><subject>A549 Cells</subject><subject>Catalytic Domain</subject><subject>Cell Line, Tumor</subject><subject>Cell Proliferation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Gene Silencing</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Phosphatase 2 - antagonists & inhibitors</subject><subject>Protein Phosphatase 2 - metabolism</subject><subject>Protein Phosphatase 2C - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Subunits - genetics</subject><subject>Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism</subject><subject>Research Paper</subject><subject>Ubiquitination</subject><issn>1949-2553</issn><issn>1949-2553</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkMFOwzAMhiMEYmjsAbigHjnQkbhJmx5AqiYGSENc4BwlTboWdUlJOhBvT7WNMXyxJf_-bX8IXRA8JTxN4MbZ0vXSL00_JSTN-RE6IznNY2AsOT6oR2gSwjsegtGMQ36KRpAxziknZ-h2XjwTgOI6kpE1X5Gx2i2NdesQNbZuVNM7H7kq6rzrTWOjrnahq2Uvg4mgOEcnlWyDmezyGL3N719nj_Hi5eFpVizikkLax0SBopjzhLIKqwynVBsFEsoKuNRZWoKWRpc60xrnWZpWSUmNYhJUBqzKdDJGd1vfbq1Wg9LY3stWdL5ZSf8tnGzE_45tarF0n4IlwCghg8HVzsC7j7UJvVg1oTRtK60ZfhWEM8oxpAkdpGQrLb0LwZtqv4ZgsSEv_siLDflh5vLwvv3EL-fkB0c_gjs</recordid><startdate>20160927</startdate><enddate>20160927</enddate><creator>Fan, Li</creator><creator>Liu, Man-Hua</creator><creator>Guo, Meng</creator><creator>Hu, Chuan-Xi</creator><creator>Yan, Zhao-Wen</creator><creator>Chen, Jing</creator><creator>Chen, Guo-Qiang</creator><creator>Huang, Ying</creator><general>Impact Journals LLC</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160927</creationdate><title>FAM122A, a new endogenous inhibitor of protein phosphatase 2A</title><author>Fan, Li ; Liu, Man-Hua ; Guo, Meng ; Hu, Chuan-Xi ; Yan, Zhao-Wen ; Chen, Jing ; Chen, Guo-Qiang ; Huang, Ying</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-1b2b4088345f0b7064deb2a2cf28ad76c2daedcd7dd09766f3c4eb5a2b725f7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>A549 Cells</topic><topic>Catalytic Domain</topic><topic>Cell Line, Tumor</topic><topic>Cell Proliferation</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Gene Silencing</topic><topic>HEK293 Cells</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Phosphatase 2 - antagonists & inhibitors</topic><topic>Protein Phosphatase 2 - metabolism</topic><topic>Protein Phosphatase 2C - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Subunits - genetics</topic><topic>Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism</topic><topic>Research Paper</topic><topic>Ubiquitination</topic><toplevel>online_resources</toplevel><creatorcontrib>Fan, Li</creatorcontrib><creatorcontrib>Liu, Man-Hua</creatorcontrib><creatorcontrib>Guo, Meng</creatorcontrib><creatorcontrib>Hu, Chuan-Xi</creatorcontrib><creatorcontrib>Yan, Zhao-Wen</creatorcontrib><creatorcontrib>Chen, Jing</creatorcontrib><creatorcontrib>Chen, Guo-Qiang</creatorcontrib><creatorcontrib>Huang, Ying</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncotarget</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fan, Li</au><au>Liu, Man-Hua</au><au>Guo, Meng</au><au>Hu, Chuan-Xi</au><au>Yan, Zhao-Wen</au><au>Chen, Jing</au><au>Chen, Guo-Qiang</au><au>Huang, Ying</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FAM122A, a new endogenous inhibitor of protein phosphatase 2A</atitle><jtitle>Oncotarget</jtitle><addtitle>Oncotarget</addtitle><date>2016-09-27</date><risdate>2016</risdate><volume>7</volume><issue>39</issue><spage>63887</spage><epage>63900</epage><pages>63887-63900</pages><issn>1949-2553</issn><eissn>1949-2553</eissn><abstract>The regulation of the ubiquitously expressed protein phosphatase 2A (PP2A) is essential for various cellular functions such as cell proliferation, transformation, and fate determination. In this study, we demonstrate that the highly conserved protein in mammals, designated FAM122A, directly interacts with PP2A-Aα and B55α rather than B56α subunits, and inhibits the phosphatase activity of PP2A-Aα/B55α/Cα complex. Further, FAM122A potentiates the degradation of catalytic subunit PP2A-Cα with the increased poly-ubiquitination. In agreement, FAM122A silencing inhibits while its overexpression enhances cell growth and colony-forming ability. Collectively, we identify FAM122A as a new endogenous PP2A inhibitor and its physiological and pathophysiological significances warrant to be further investigated.</abstract><cop>United States</cop><pub>Impact Journals LLC</pub><pmid>27588481</pmid><doi>10.18632/oncotarget.11698</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | A549 Cells Catalytic Domain Cell Line, Tumor Cell Proliferation Enzyme Inhibitors - pharmacology Gene Expression Regulation, Neoplastic Gene Silencing HEK293 Cells HeLa Cells Humans Phosphoproteins - genetics Phosphoproteins - metabolism Phosphorylation Protein Binding Protein Phosphatase 2 - antagonists & inhibitors Protein Phosphatase 2 - metabolism Protein Phosphatase 2C - metabolism Protein Processing, Post-Translational Protein Subunits - genetics Receptor-Like Protein Tyrosine Phosphatases, Class 2 - metabolism Research Paper Ubiquitination |
| title | FAM122A, a new endogenous inhibitor of protein phosphatase 2A |
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