The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity
The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-01, Vol.92 (1), p.112-116 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Skinner, H.B. (University of Alabama, Birmingham, AL.) McGee, T.P McMaster, C.R Fry, M.R Bell, R.M Bankaitis, V.A |
| description | The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14p function and the CDP-choline pathway has remained obscure. We now report that SEC14p effects an in vivo depression of CDP-choline pathway activity by inhibiting choline-phosphate cytidylyltransferase (CCTase; EC 2.7.7.15), the rate-determining enzyme of the CDP-choline pathway. Moreover, this SEC14p-mediated inhibition of CCTase was recapitulated in vitro and was saturable. Finally, whereas the SEC14p-dependent inhibition of CCTase in vitro was markedly reduced under assay conditions that were expected to increase levels of phosphatidylinositol-bound SEC14p, assay conditions expected to increase levels of phosphatidylcholine-bound SEC14p resulted in significant potentiation of CCTase inhibition. The collective data suggest that the phosphatidylcholine-bound form of SEC14p effects an essential repression of CDP-choline pathway activity in Golgi membranes by inhibiting CCTase and that the phospholipid-binding/exchange activity of SEC14p represents a mechanism by which the regulatory activity of SEC14p is itself controlled |
| doi_str_mv | 10.1073/pnas.92.1.112 |
| format | Article |
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(University of Alabama, Birmingham, AL.) ; McGee, T.P ; McMaster, C.R ; Fry, M.R ; Bell, R.M ; Bankaitis, V.A</creator><creatorcontrib>Skinner, H.B. (University of Alabama, Birmingham, AL.) ; McGee, T.P ; McMaster, C.R ; Fry, M.R ; Bell, R.M ; Bankaitis, V.A</creatorcontrib><description>The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14p function and the CDP-choline pathway has remained obscure. We now report that SEC14p effects an in vivo depression of CDP-choline pathway activity by inhibiting choline-phosphate cytidylyltransferase (CCTase; EC 2.7.7.15), the rate-determining enzyme of the CDP-choline pathway. Moreover, this SEC14p-mediated inhibition of CCTase was recapitulated in vitro and was saturable. Finally, whereas the SEC14p-dependent inhibition of CCTase in vitro was markedly reduced under assay conditions that were expected to increase levels of phosphatidylinositol-bound SEC14p, assay conditions expected to increase levels of phosphatidylcholine-bound SEC14p resulted in significant potentiation of CCTase inhibition. The collective data suggest that the phosphatidylcholine-bound form of SEC14p effects an essential repression of CDP-choline pathway activity in Golgi membranes by inhibiting CCTase and that the phospholipid-binding/exchange activity of SEC14p represents a mechanism by which the regulatory activity of SEC14p is itself controlled</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.1.112</identifier><identifier>PMID: 7816798</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; APARATO GOLGI ; APPAREIL DE GOLGI ; Carbon Radioisotopes ; Carrier Proteins - biosynthesis ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Cell biology ; Cells ; Choline - metabolism ; Choline-Phosphate Cytidylyltransferase ; Cloning, Molecular ; Cytidine Diphosphate Choline - metabolism ; Cytosol - metabolism ; Enzymes ; Escherichia coli ; FOSFOLIPIDOS ; Genotype ; Golgi Apparatus - metabolism ; INHIBICION ; INHIBITION ; Intracellular Membranes - metabolism ; Kinetics ; Ligands ; Lipids ; MEMBRANAS CELULARES ; MEMBRANE CELLULAIRE ; Membrane Proteins ; Models, Biological ; Nucleotidyltransferases - antagonists & inhibitors ; Overproduction ; P branes ; PHOSPHATIDE ; Phosphatidylinositols - metabolism ; Phospholipid Transfer Proteins ; Phospholipids ; Phospholipids - isolation & purification ; Phospholipids - metabolism ; PROTEINAS ; PROTEINAS AGLUTINANTES ; PROTEINE ; PROTEINE DE LIAISON ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Repression ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Sensors ; TRANSFERASAS ; TRANSFERASE ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-01, Vol.92 (1), p.112-116</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c568t-fe420ad2b18a263a42957695a601406efce926473b54dc58741cf2a5189a6cf43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2366509$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2366509$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53770,53772,57996,58229</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7816798$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Skinner, H.B. (University of Alabama, Birmingham, AL.)</creatorcontrib><creatorcontrib>McGee, T.P</creatorcontrib><creatorcontrib>McMaster, C.R</creatorcontrib><creatorcontrib>Fry, M.R</creatorcontrib><creatorcontrib>Bell, R.M</creatorcontrib><creatorcontrib>Bankaitis, V.A</creatorcontrib><title>The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14p function and the CDP-choline pathway has remained obscure. We now report that SEC14p effects an in vivo depression of CDP-choline pathway activity by inhibiting choline-phosphate cytidylyltransferase (CCTase; EC 2.7.7.15), the rate-determining enzyme of the CDP-choline pathway. Moreover, this SEC14p-mediated inhibition of CCTase was recapitulated in vitro and was saturable. Finally, whereas the SEC14p-dependent inhibition of CCTase in vitro was markedly reduced under assay conditions that were expected to increase levels of phosphatidylinositol-bound SEC14p, assay conditions expected to increase levels of phosphatidylcholine-bound SEC14p resulted in significant potentiation of CCTase inhibition. The collective data suggest that the phosphatidylcholine-bound form of SEC14p effects an essential repression of CDP-choline pathway activity in Golgi membranes by inhibiting CCTase and that the phospholipid-binding/exchange activity of SEC14p represents a mechanism by which the regulatory activity of SEC14p is itself controlled</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>APARATO GOLGI</subject><subject>APPAREIL DE GOLGI</subject><subject>Carbon Radioisotopes</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell biology</subject><subject>Cells</subject><subject>Choline - metabolism</subject><subject>Choline-Phosphate Cytidylyltransferase</subject><subject>Cloning, Molecular</subject><subject>Cytidine Diphosphate Choline - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>FOSFOLIPIDOS</subject><subject>Genotype</subject><subject>Golgi Apparatus - metabolism</subject><subject>INHIBICION</subject><subject>INHIBITION</subject><subject>Intracellular Membranes - metabolism</subject><subject>Kinetics</subject><subject>Ligands</subject><subject>Lipids</subject><subject>MEMBRANAS CELULARES</subject><subject>MEMBRANE CELLULAIRE</subject><subject>Membrane Proteins</subject><subject>Models, Biological</subject><subject>Nucleotidyltransferases - antagonists & inhibitors</subject><subject>Overproduction</subject><subject>P branes</subject><subject>PHOSPHATIDE</subject><subject>Phosphatidylinositols - metabolism</subject><subject>Phospholipid Transfer Proteins</subject><subject>Phospholipids</subject><subject>Phospholipids - isolation & purification</subject><subject>Phospholipids - metabolism</subject><subject>PROTEINAS</subject><subject>PROTEINAS AGLUTINANTES</subject><subject>PROTEINE</subject><subject>PROTEINE DE LIAISON</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Repression</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sensors</subject><subject>TRANSFERASAS</subject><subject>TRANSFERASE</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhSMEKqWwZINA8gZ2GWwndmKpG1TxkiqxaLu27jjXE1cZO9ieEfkt_FkyzIOygdVdfOccnatTFC8ZXTDaVO9HD2mh-IItGOOPinNGFStlrejj4pxS3pRtzeunxbOU7imlSrT0rDhrWiYb1Z4XP297JDdgTA8xrCeDiRiMuHXJAZKxD2nsIbtuGpwPyeUwlDmCTxYjGWPI6DxBa9HkRIAMbgW-Kzsc0XfoM3G-d0uXXfAkWGL6MMdgeYxFYqbf2dNwDIWEBEx2W5en58UTC0PCF4d7Udx9-nh79aW8_vb569WH69II2ebSYs0pdHzJWuCygpor0UglQFJWU4nWoOKybqqlqDsj2qZmxnIQrFUgja2ri-JynztulmvszFw8wqDH6NYQJx3A6b-Jd71eha2uecub2f7uYI_h-wZT1muXDA4DeAybpJuG8YqK6r_CeRLBpNwVKvdCE0NKEe2pC6N6N7reja4V10zPo8_6Nw8fOKkPK8_89YHvbEf6wP72H1jbzTBk_JH_xNynHOJJyCspBVUzfrXHFoKGVXRJ390oUQkxP_8LeQDXjw</recordid><startdate>19950103</startdate><enddate>19950103</enddate><creator>Skinner, H.B. (University of Alabama, Birmingham, AL.)</creator><creator>McGee, T.P</creator><creator>McMaster, C.R</creator><creator>Fry, M.R</creator><creator>Bell, R.M</creator><creator>Bankaitis, V.A</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</scope><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>M7N</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950103</creationdate><title>The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity</title><author>Skinner, H.B. (University of Alabama, Birmingham, AL.) ; McGee, T.P ; McMaster, C.R ; Fry, M.R ; Bell, R.M ; Bankaitis, V.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c568t-fe420ad2b18a263a42957695a601406efce926473b54dc58741cf2a5189a6cf43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>APARATO GOLGI</topic><topic>APPAREIL DE GOLGI</topic><topic>Carbon Radioisotopes</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell biology</topic><topic>Cells</topic><topic>Choline - metabolism</topic><topic>Choline-Phosphate Cytidylyltransferase</topic><topic>Cloning, Molecular</topic><topic>Cytidine Diphosphate Choline - metabolism</topic><topic>Cytosol - metabolism</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>FOSFOLIPIDOS</topic><topic>Genotype</topic><topic>Golgi Apparatus - metabolism</topic><topic>INHIBICION</topic><topic>INHIBITION</topic><topic>Intracellular Membranes - metabolism</topic><topic>Kinetics</topic><topic>Ligands</topic><topic>Lipids</topic><topic>MEMBRANAS CELULARES</topic><topic>MEMBRANE CELLULAIRE</topic><topic>Membrane Proteins</topic><topic>Models, Biological</topic><topic>Nucleotidyltransferases - antagonists & inhibitors</topic><topic>Overproduction</topic><topic>P branes</topic><topic>PHOSPHATIDE</topic><topic>Phosphatidylinositols - metabolism</topic><topic>Phospholipid Transfer Proteins</topic><topic>Phospholipids</topic><topic>Phospholipids - isolation & purification</topic><topic>Phospholipids - metabolism</topic><topic>PROTEINAS</topic><topic>PROTEINAS AGLUTINANTES</topic><topic>PROTEINE</topic><topic>PROTEINE DE LIAISON</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Repression</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sensors</topic><topic>TRANSFERASAS</topic><topic>TRANSFERASE</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Skinner, H.B. (University of Alabama, Birmingham, AL.)</creatorcontrib><creatorcontrib>McGee, T.P</creatorcontrib><creatorcontrib>McMaster, C.R</creatorcontrib><creatorcontrib>Fry, M.R</creatorcontrib><creatorcontrib>Bell, R.M</creatorcontrib><creatorcontrib>Bankaitis, V.A</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Skinner, H.B. (University of Alabama, Birmingham, AL.)</au><au>McGee, T.P</au><au>McMaster, C.R</au><au>Fry, M.R</au><au>Bell, R.M</au><au>Bankaitis, V.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-01-03</date><risdate>1995</risdate><volume>92</volume><issue>1</issue><spage>112</spage><epage>116</epage><pages>112-116</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Saccharomyces cerevisiae protein SEC14p is required for Golgi function and cell viability in vivo. This requirement is obviated by mutations that specifically inactivate the CDP-choline pathway for phosphatidylcholine biosynthesis. The biochemical basis for the in vivo relationship between SEC14p function and the CDP-choline pathway has remained obscure. We now report that SEC14p effects an in vivo depression of CDP-choline pathway activity by inhibiting choline-phosphate cytidylyltransferase (CCTase; EC 2.7.7.15), the rate-determining enzyme of the CDP-choline pathway. Moreover, this SEC14p-mediated inhibition of CCTase was recapitulated in vitro and was saturable. Finally, whereas the SEC14p-dependent inhibition of CCTase in vitro was markedly reduced under assay conditions that were expected to increase levels of phosphatidylinositol-bound SEC14p, assay conditions expected to increase levels of phosphatidylcholine-bound SEC14p resulted in significant potentiation of CCTase inhibition. The collective data suggest that the phosphatidylcholine-bound form of SEC14p effects an essential repression of CDP-choline pathway activity in Golgi membranes by inhibiting CCTase and that the phospholipid-binding/exchange activity of SEC14p represents a mechanism by which the regulatory activity of SEC14p is itself controlled</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7816798</pmid><doi>10.1073/pnas.92.1.112</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1995-01, Vol.92 (1), p.112-116 |
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| subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE APARATO GOLGI APPAREIL DE GOLGI Carbon Radioisotopes Carrier Proteins - biosynthesis Carrier Proteins - isolation & purification Carrier Proteins - metabolism Cell biology Cells Choline - metabolism Choline-Phosphate Cytidylyltransferase Cloning, Molecular Cytidine Diphosphate Choline - metabolism Cytosol - metabolism Enzymes Escherichia coli FOSFOLIPIDOS Genotype Golgi Apparatus - metabolism INHIBICION INHIBITION Intracellular Membranes - metabolism Kinetics Ligands Lipids MEMBRANAS CELULARES MEMBRANE CELLULAIRE Membrane Proteins Models, Biological Nucleotidyltransferases - antagonists & inhibitors Overproduction P branes PHOSPHATIDE Phosphatidylinositols - metabolism Phospholipid Transfer Proteins Phospholipids Phospholipids - isolation & purification Phospholipids - metabolism PROTEINAS PROTEINAS AGLUTINANTES PROTEINE PROTEINE DE LIAISON Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Repression SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Sensors TRANSFERASAS TRANSFERASE Yeasts |
| title | The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity |
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