Human ABCC1 Interacts and Colocalizes with ATP Synthase α, Revealed by Interactive Proteomics Analysis
Human ABCC1 is a member of the ATP-binding cassette (ABC) transporter superfamily, and its overexpression has been shown to cause multidrug resistance by active efflux of a wide variety of anticancer drugs. ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heter...
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| Veröffentlicht in: | Journal of proteome research 2012-02, Vol.11 (2), p.1364-1372 |
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| container_title | Journal of proteome research |
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| creator | Yang, Youyun Li, Zhaomin Mo, Wei Ambadipudi, Raghuram Arnold, Randy J Hrncirova, Petra Novotny, Milos V Georges, Elias Zhang, Jian-Ting |
| description | Human ABCC1 is a member of the ATP-binding cassette (ABC) transporter superfamily, and its overexpression has been shown to cause multidrug resistance by active efflux of a wide variety of anticancer drugs. ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heterocomplex involving ABCC1 has been indicated. In this study, we performed an interactive proteomics study to examine proteins that bind to and form heterocomplexes with ABCC1 using coimmunoprecipitation and tandem mass spectrometry (MS/MS) analyses. We found that ATP synthase α binds to ABCC1 in plasma membranes with a ratio of 2:1. The ATP synthase α binding site in ABCC1 is located in the linker domain at the carboxyl core of ABCC1, and phosphorylation of the linker domain at the protein kinase A site enhances ATP synthase α binding. The interaction between ABCC1 and ATP synthase α in a heterocomplex may indicate a novel function of ABCC1 in regulating extracellular ATP level and purinergic signaling cascade. |
| doi_str_mv | 10.1021/pr201003g |
| format | Article |
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ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heterocomplex involving ABCC1 has been indicated. In this study, we performed an interactive proteomics study to examine proteins that bind to and form heterocomplexes with ABCC1 using coimmunoprecipitation and tandem mass spectrometry (MS/MS) analyses. We found that ATP synthase α binds to ABCC1 in plasma membranes with a ratio of 2:1. The ATP synthase α binding site in ABCC1 is located in the linker domain at the carboxyl core of ABCC1, and phosphorylation of the linker domain at the protein kinase A site enhances ATP synthase α binding. The interaction between ABCC1 and ATP synthase α in a heterocomplex may indicate a novel function of ABCC1 in regulating extracellular ATP level and purinergic signaling cascade.</description><identifier>ISSN: 1535-3893</identifier><identifier>EISSN: 1535-3907</identifier><identifier>DOI: 10.1021/pr201003g</identifier><identifier>PMID: 22188235</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Binding Sites ; HEK293 Cells ; Humans ; Immunoprecipitation ; Mitochondrial Proton-Translocating ATPases - chemistry ; Mitochondrial Proton-Translocating ATPases - metabolism ; Models, Biological ; Molecular Sequence Data ; Multidrug Resistance-Associated Proteins - chemistry ; Multidrug Resistance-Associated Proteins - metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Mapping - methods ; Proteomics - methods ; Reproducibility of Results</subject><ispartof>Journal of proteome research, 2012-02, Vol.11 (2), p.1364-1372</ispartof><rights>Copyright © 2011 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a404t-2153d6491c9d5388fed83fbb2b59d981374097bbcf4f1047454b1319eca2ef393</citedby><cites>FETCH-LOGICAL-a404t-2153d6491c9d5388fed83fbb2b59d981374097bbcf4f1047454b1319eca2ef393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/pr201003g$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/pr201003g$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22188235$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Youyun</creatorcontrib><creatorcontrib>Li, Zhaomin</creatorcontrib><creatorcontrib>Mo, Wei</creatorcontrib><creatorcontrib>Ambadipudi, Raghuram</creatorcontrib><creatorcontrib>Arnold, Randy J</creatorcontrib><creatorcontrib>Hrncirova, Petra</creatorcontrib><creatorcontrib>Novotny, Milos V</creatorcontrib><creatorcontrib>Georges, Elias</creatorcontrib><creatorcontrib>Zhang, Jian-Ting</creatorcontrib><title>Human ABCC1 Interacts and Colocalizes with ATP Synthase α, Revealed by Interactive Proteomics Analysis</title><title>Journal of proteome research</title><addtitle>J. Proteome Res</addtitle><description>Human ABCC1 is a member of the ATP-binding cassette (ABC) transporter superfamily, and its overexpression has been shown to cause multidrug resistance by active efflux of a wide variety of anticancer drugs. ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heterocomplex involving ABCC1 has been indicated. In this study, we performed an interactive proteomics study to examine proteins that bind to and form heterocomplexes with ABCC1 using coimmunoprecipitation and tandem mass spectrometry (MS/MS) analyses. We found that ATP synthase α binds to ABCC1 in plasma membranes with a ratio of 2:1. The ATP synthase α binding site in ABCC1 is located in the linker domain at the carboxyl core of ABCC1, and phosphorylation of the linker domain at the protein kinase A site enhances ATP synthase α binding. The interaction between ABCC1 and ATP synthase α in a heterocomplex may indicate a novel function of ABCC1 in regulating extracellular ATP level and purinergic signaling cascade.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Mitochondrial Proton-Translocating ATPases - chemistry</subject><subject>Mitochondrial Proton-Translocating ATPases - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Multidrug Resistance-Associated Proteins - chemistry</subject><subject>Multidrug Resistance-Associated Proteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Interaction Mapping - methods</subject><subject>Proteomics - methods</subject><subject>Reproducibility of Results</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1KAzEQx4MotlYPvoDk4kFwNV_rJhdhXdQWChat55DNZtuU_SjJtrK-lS_iM7lSWxQ8zcD85jfDH4BTjK4wIvh66QjCCNHZHujjkIYBFSja3_Zc0B448n6BEA4jRA9BjxDMOaFhH8yGq1JVML5LEgxHVWOc0o2HqspgUhe1VoV9Nx6-2WYO4-kEvrRVM1fewM-PS_hs1kYVJoNpu9u1awMnrm5MXVrtYVypovXWH4ODXBXenPzUAXh9uJ8mw2D89DhK4nGgGGJNQLqXsxsmsBZZSDnPTcZpnqYkDUUmOKYRQyJKU52zHCMWsZClmGJhtCImp4IOwO3Gu1ylpcm0qRqnCrl0tlSulbWy8u-ksnM5q9eSE04Fw53gYiPQrvbemXy3i5H8Tlvu0u7Ys9_HduQ23g443wBKe7moV65Lw_8j-gI3dof0</recordid><startdate>20120203</startdate><enddate>20120203</enddate><creator>Yang, Youyun</creator><creator>Li, Zhaomin</creator><creator>Mo, Wei</creator><creator>Ambadipudi, Raghuram</creator><creator>Arnold, Randy J</creator><creator>Hrncirova, Petra</creator><creator>Novotny, Milos V</creator><creator>Georges, Elias</creator><creator>Zhang, Jian-Ting</creator><general>American Chemical Society</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>20120203</creationdate><title>Human ABCC1 Interacts and Colocalizes with ATP Synthase α, Revealed by Interactive Proteomics Analysis</title><author>Yang, Youyun ; Li, Zhaomin ; Mo, Wei ; Ambadipudi, Raghuram ; Arnold, Randy J ; Hrncirova, Petra ; Novotny, Milos V ; Georges, Elias ; Zhang, Jian-Ting</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a404t-2153d6491c9d5388fed83fbb2b59d981374097bbcf4f1047454b1319eca2ef393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Mitochondrial Proton-Translocating ATPases - chemistry</topic><topic>Mitochondrial Proton-Translocating ATPases - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Multidrug Resistance-Associated Proteins - chemistry</topic><topic>Multidrug Resistance-Associated Proteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Interaction Mapping - methods</topic><topic>Proteomics - methods</topic><topic>Reproducibility of Results</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Youyun</creatorcontrib><creatorcontrib>Li, Zhaomin</creatorcontrib><creatorcontrib>Mo, Wei</creatorcontrib><creatorcontrib>Ambadipudi, Raghuram</creatorcontrib><creatorcontrib>Arnold, Randy J</creatorcontrib><creatorcontrib>Hrncirova, Petra</creatorcontrib><creatorcontrib>Novotny, Milos V</creatorcontrib><creatorcontrib>Georges, Elias</creatorcontrib><creatorcontrib>Zhang, Jian-Ting</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>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Youyun</au><au>Li, Zhaomin</au><au>Mo, Wei</au><au>Ambadipudi, Raghuram</au><au>Arnold, Randy J</au><au>Hrncirova, Petra</au><au>Novotny, Milos V</au><au>Georges, Elias</au><au>Zhang, Jian-Ting</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human ABCC1 Interacts and Colocalizes with ATP Synthase α, Revealed by Interactive Proteomics Analysis</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2012-02-03</date><risdate>2012</risdate><volume>11</volume><issue>2</issue><spage>1364</spage><epage>1372</epage><pages>1364-1372</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>Human ABCC1 is a member of the ATP-binding cassette (ABC) transporter superfamily, and its overexpression has been shown to cause multidrug resistance by active efflux of a wide variety of anticancer drugs. ABCC1 has been shown to exist and possibly function as a homodimer. However, a possible heterocomplex involving ABCC1 has been indicated. In this study, we performed an interactive proteomics study to examine proteins that bind to and form heterocomplexes with ABCC1 using coimmunoprecipitation and tandem mass spectrometry (MS/MS) analyses. We found that ATP synthase α binds to ABCC1 in plasma membranes with a ratio of 2:1. The ATP synthase α binding site in ABCC1 is located in the linker domain at the carboxyl core of ABCC1, and phosphorylation of the linker domain at the protein kinase A site enhances ATP synthase α binding. The interaction between ABCC1 and ATP synthase α in a heterocomplex may indicate a novel function of ABCC1 in regulating extracellular ATP level and purinergic signaling cascade.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>22188235</pmid><doi>10.1021/pr201003g</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Amino Acid Sequence Binding Sites HEK293 Cells Humans Immunoprecipitation Mitochondrial Proton-Translocating ATPases - chemistry Mitochondrial Proton-Translocating ATPases - metabolism Models, Biological Molecular Sequence Data Multidrug Resistance-Associated Proteins - chemistry Multidrug Resistance-Associated Proteins - metabolism Phosphorylation Protein Binding Protein Interaction Mapping - methods Proteomics - methods Reproducibility of Results |
| title | Human ABCC1 Interacts and Colocalizes with ATP Synthase α, Revealed by Interactive Proteomics Analysis |
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