Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells
Protein phosphatase 2A (PP2A) is a ubiquitous phospho-serine/threonine phosphatase that controls many diverse cellular functions. The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subun...
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| creator | Mo, Shu-Ting Chiang, Shang-Ju Lai, Tai-Yu Cheng, Yu-Ling Chung, Cheng-En Kuo, Spencer C H Reece, Kelie M Chen, Yung-Cheng Chang, Nan-Shan Wadzinski, Brian E Chiang, Chi-Wu |
| description | Protein phosphatase 2A (PP2A) is a ubiquitous phospho-serine/threonine phosphatase that controls many diverse cellular functions. The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subunit also associates with other interacting partners, such as α4, to form non-canonical PP2A complexes. We report visualization of PP2A complexes in mammalian cells. Bimolecular fluorescence complementation (BiFC) analysis of PP2A subunit interactions demonstrates that the B subunit plays a key role in directing the subcellular localization of PP2A, and confirms that the A subunit functions as a scaffold in recruiting the B and C subunits to form a heterotrimeric holoenzyme. BiFC analysis also reveals that α4 promotes formation of the AC core dimer. Furthermore, we demonstrate visualization of specific ABC holoenzymes in cells by combining BiFC and fluorescence resonance energy transfer (BiFC-FRET). Our studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP2A complexes in cells. |
| doi_str_mv | 10.1371/journal.pone.0116074 |
| format | Article |
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The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subunit also associates with other interacting partners, such as α4, to form non-canonical PP2A complexes. We report visualization of PP2A complexes in mammalian cells. Bimolecular fluorescence complementation (BiFC) analysis of PP2A subunit interactions demonstrates that the B subunit plays a key role in directing the subcellular localization of PP2A, and confirms that the A subunit functions as a scaffold in recruiting the B and C subunits to form a heterotrimeric holoenzyme. BiFC analysis also reveals that α4 promotes formation of the AC core dimer. Furthermore, we demonstrate visualization of specific ABC holoenzymes in cells by combining BiFC and fluorescence resonance energy transfer (BiFC-FRET). Our studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP2A complexes in cells.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0116074</identifier><identifier>PMID: 25536081</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Antigens ; Biochemistry ; Biology and Life Sciences ; Catalysis ; Cell cycle ; Cells (Biology) ; Energy transfer ; Enzymes ; Fluorescence ; Fluorescence resonance energy transfer ; Fluorescent Antibody Technique ; Infectious diseases ; Kinases ; Localization ; Mammalian cells ; Mammals ; Medicine ; Mice ; NIH 3T3 Cells ; Phosphatase ; Phosphatases ; Phosphoprotein phosphatase ; Physical Sciences ; Protein Multimerization ; Protein phosphatase ; Protein Phosphatase 2 - analysis ; Protein Phosphatase 2 - metabolism ; Protein Subunits - analysis ; Protein Subunits - metabolism ; Protein-serine/threonine phosphatase ; Proteins ; Regulation ; Research and Analysis Methods ; Scaffolding ; Serine ; Signal transduction ; Spatial distribution ; Temporal distribution ; Threonine ; Threonine phosphatase ; Visualization ; Yeast</subject><ispartof>PloS one, 2014-12, Vol.9 (12), p.e116074-e116074</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Mo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Mo et al 2014 Mo et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c762t-b9b5dc98c1775e430f429e9116e7c68f3532bd6b794be27ef6ae4e0c1b8af2853</citedby><cites>FETCH-LOGICAL-c762t-b9b5dc98c1775e430f429e9116e7c68f3532bd6b794be27ef6ae4e0c1b8af2853</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/PMC4275284/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4275284/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25536081$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Janssens, Veerle</contributor><creatorcontrib>Mo, Shu-Ting</creatorcontrib><creatorcontrib>Chiang, Shang-Ju</creatorcontrib><creatorcontrib>Lai, Tai-Yu</creatorcontrib><creatorcontrib>Cheng, Yu-Ling</creatorcontrib><creatorcontrib>Chung, Cheng-En</creatorcontrib><creatorcontrib>Kuo, Spencer C H</creatorcontrib><creatorcontrib>Reece, Kelie M</creatorcontrib><creatorcontrib>Chen, Yung-Cheng</creatorcontrib><creatorcontrib>Chang, Nan-Shan</creatorcontrib><creatorcontrib>Wadzinski, Brian E</creatorcontrib><creatorcontrib>Chiang, Chi-Wu</creatorcontrib><title>Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Protein phosphatase 2A (PP2A) is a ubiquitous phospho-serine/threonine phosphatase that controls many diverse cellular functions. The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subunit also associates with other interacting partners, such as α4, to form non-canonical PP2A complexes. We report visualization of PP2A complexes in mammalian cells. Bimolecular fluorescence complementation (BiFC) analysis of PP2A subunit interactions demonstrates that the B subunit plays a key role in directing the subcellular localization of PP2A, and confirms that the A subunit functions as a scaffold in recruiting the B and C subunits to form a heterotrimeric holoenzyme. BiFC analysis also reveals that α4 promotes formation of the AC core dimer. Furthermore, we demonstrate visualization of specific ABC holoenzymes in cells by combining BiFC and fluorescence resonance energy transfer (BiFC-FRET). Our studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP2A complexes in cells.</description><subject>Animals</subject><subject>Antigens</subject><subject>Biochemistry</subject><subject>Biology and Life Sciences</subject><subject>Catalysis</subject><subject>Cell cycle</subject><subject>Cells (Biology)</subject><subject>Energy transfer</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Fluorescence resonance energy transfer</subject><subject>Fluorescent Antibody Technique</subject><subject>Infectious diseases</subject><subject>Kinases</subject><subject>Localization</subject><subject>Mammalian cells</subject><subject>Mammals</subject><subject>Medicine</subject><subject>Mice</subject><subject>NIH 3T3 Cells</subject><subject>Phosphatase</subject><subject>Phosphatases</subject><subject>Phosphoprotein 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of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells</title><author>Mo, Shu-Ting ; Chiang, Shang-Ju ; Lai, Tai-Yu ; Cheng, Yu-Ling ; Chung, Cheng-En ; Kuo, Spencer C H ; Reece, Kelie M ; Chen, Yung-Cheng ; Chang, Nan-Shan ; Wadzinski, Brian E ; Chiang, Chi-Wu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c762t-b9b5dc98c1775e430f429e9116e7c68f3532bd6b794be27ef6ae4e0c1b8af2853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animals</topic><topic>Antigens</topic><topic>Biochemistry</topic><topic>Biology and Life Sciences</topic><topic>Catalysis</topic><topic>Cell cycle</topic><topic>Cells (Biology)</topic><topic>Energy transfer</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Fluorescence resonance energy transfer</topic><topic>Fluorescent Antibody Technique</topic><topic>Infectious 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One</addtitle><date>2014-12-23</date><risdate>2014</risdate><volume>9</volume><issue>12</issue><spage>e116074</spage><epage>e116074</epage><pages>e116074-e116074</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Protein phosphatase 2A (PP2A) is a ubiquitous phospho-serine/threonine phosphatase that controls many diverse cellular functions. The predominant form of PP2A is a heterotrimeric holoenzyme consisting of a scaffolding A subunit, a variable regulatory B subunit, and a catalytic C subunit. The C subunit also associates with other interacting partners, such as α4, to form non-canonical PP2A complexes. We report visualization of PP2A complexes in mammalian cells. Bimolecular fluorescence complementation (BiFC) analysis of PP2A subunit interactions demonstrates that the B subunit plays a key role in directing the subcellular localization of PP2A, and confirms that the A subunit functions as a scaffold in recruiting the B and C subunits to form a heterotrimeric holoenzyme. BiFC analysis also reveals that α4 promotes formation of the AC core dimer. Furthermore, we demonstrate visualization of specific ABC holoenzymes in cells by combining BiFC and fluorescence resonance energy transfer (BiFC-FRET). Our studies not only provide direct imaging data to support previous biochemical observations on PP2A complexes, but also offer a promising approach for studying the spatiotemporal distribution of individual PP2A complexes in cells.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25536081</pmid><doi>10.1371/journal.pone.0116074</doi><oa>free_for_read</oa></addata></record> |
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| issn | 1932-6203 1932-6203 |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Antigens Biochemistry Biology and Life Sciences Catalysis Cell cycle Cells (Biology) Energy transfer Enzymes Fluorescence Fluorescence resonance energy transfer Fluorescent Antibody Technique Infectious diseases Kinases Localization Mammalian cells Mammals Medicine Mice NIH 3T3 Cells Phosphatase Phosphatases Phosphoprotein phosphatase Physical Sciences Protein Multimerization Protein phosphatase Protein Phosphatase 2 - analysis Protein Phosphatase 2 - metabolism Protein Subunits - analysis Protein Subunits - metabolism Protein-serine/threonine phosphatase Proteins Regulation Research and Analysis Methods Scaffolding Serine Signal transduction Spatial distribution Temporal distribution Threonine Threonine phosphatase Visualization Yeast |
| title | Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T05%3A03%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Visualization%20of%20subunit%20interactions%20and%20ternary%20complexes%20of%20protein%20phosphatase%202A%20in%20mammalian%20cells&rft.jtitle=PloS%20one&rft.au=Mo,%20Shu-Ting&rft.date=2014-12-23&rft.volume=9&rft.issue=12&rft.spage=e116074&rft.epage=e116074&rft.pages=e116074-e116074&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0116074&rft_dat=%3Cgale_plos_%3EA418126328%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1640007268&rft_id=info:pmid/25536081&rft_galeid=A418126328&rft_doaj_id=oai_doaj_org_article_fec58042bd05488b82ad7f64834f6625&rfr_iscdi=true |