Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast
The rapamycin·FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+-ATPase. Deleting PMR1 in two genetic backgrounds...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2006-11, Vol.103 (47), p.17840-17845 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Devasahayam, G Ritz, D Helliwell, S.B Burke, D.J Sturgill, T.W |
| description | The rapamycin·FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+-ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling. |
| doi_str_mv | 10.1073/pnas.0604303103 |
| format | Article |
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We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+-ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0604303103</identifier><identifier>PMID: 17095607</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>adenosinetriphosphatase ; Amino Acid Transport Systems - genetics ; Amino Acid Transport Systems - metabolism ; Antifungal Agents - metabolism ; Biological Sciences ; Ca/Mn-transpoting ATPase ; calcium ; Calcium-Transporting ATPases - genetics ; Calcium-Transporting ATPases - metabolism ; Cell growth ; Cell membranes ; Cell nucleus ; DNA ; drug resistance ; Epistasis, Genetic ; Gene expression regulation ; Gene Expression Regulation, Fungal ; Genes ; Genetics ; Golgi apparatus ; Golgi Apparatus - enzymology ; Kinases ; manganese ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; mutants ; Nitrogen ; Phenotypes ; Physiological regulation ; Plasmids ; PMR1 gene ; protein kinases ; Protein Kinases - genetics ; Protein Kinases - metabolism ; Protein Serine-Threonine Kinases ; protein transport ; rapamycin resistance ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Signal Transduction - physiology ; Sirolimus - metabolism ; target of rapamycin kinase ; Transcription Factors - metabolism ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2006-11, Vol.103 (47), p.17840-17845</ispartof><rights>Copyright 2006 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 21, 2006</rights><rights>2006 by The National Academy of Sciences of the USA 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/103/47.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30052550$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30052550$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17095607$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Devasahayam, G</creatorcontrib><creatorcontrib>Ritz, D</creatorcontrib><creatorcontrib>Helliwell, S.B</creatorcontrib><creatorcontrib>Burke, D.J</creatorcontrib><creatorcontrib>Sturgill, T.W</creatorcontrib><title>Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The rapamycin·FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+-ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling.</description><subject>adenosinetriphosphatase</subject><subject>Amino Acid Transport Systems - genetics</subject><subject>Amino Acid Transport Systems - metabolism</subject><subject>Antifungal Agents - metabolism</subject><subject>Biological Sciences</subject><subject>Ca/Mn-transpoting ATPase</subject><subject>calcium</subject><subject>Calcium-Transporting ATPases - genetics</subject><subject>Calcium-Transporting ATPases - metabolism</subject><subject>Cell growth</subject><subject>Cell membranes</subject><subject>Cell nucleus</subject><subject>DNA</subject><subject>drug resistance</subject><subject>Epistasis, Genetic</subject><subject>Gene expression regulation</subject><subject>Gene Expression Regulation, Fungal</subject><subject>Genes</subject><subject>Genetics</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - enzymology</subject><subject>Kinases</subject><subject>manganese</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - metabolism</subject><subject>mutants</subject><subject>Nitrogen</subject><subject>Phenotypes</subject><subject>Physiological regulation</subject><subject>Plasmids</subject><subject>PMR1 gene</subject><subject>protein kinases</subject><subject>Protein Kinases - genetics</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Serine-Threonine Kinases</subject><subject>protein transport</subject><subject>rapamycin resistance</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal Transduction - physiology</subject><subject>Sirolimus - metabolism</subject><subject>target of rapamycin kinase</subject><subject>Transcription Factors - metabolism</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhSMEokNhzQqwWCCqNu31I46zQapGUJCKWsF0bd1JnIxHedV2aOff49EM5bFhZVvn0_G59yTJSwqnFHJ-NvboT0GC4MAp8EfJjEJBUykKeJzMAFieKsHEQfLM-zUAFJmCp8kBzeNNQj5L1tedoycEycXQNpbMkR2ffe3ZcXq-uEZvToj1UXSmmVoMgyNDTcLKkICuMWH7cjhityltT94vrr4dEW-bHlvbN2TEsLrDDYnSxqAPz5MnNbbevNifh8nNp4-L-ef08uriy_z8Mq05kyHlVWYqlUtQzNBKLLniCoUBlEpWyIpaFZhXy7pUhcgFK7MqW9ZxFiwZq5ai4ofJh53vOC07U5WmDw5bPTrbodvoAa3-W-ntSjfDD01lET8T0eDd3sANt5PxQXfWl6ZtsTfD5LVUNM-5ZBF8-w-4HiYXx_eaAeVKFopH6PWfcR5y_OogAmQPxDJ_y8C1yCOlBETk6D-Irqe2DeY-RPbVjl37WNgDzAEylmVbrzc7vcZBY-Os1zfft3EB4tIzyvhP8reyvw</recordid><startdate>20061121</startdate><enddate>20061121</enddate><creator>Devasahayam, G</creator><creator>Ritz, D</creator><creator>Helliwell, S.B</creator><creator>Burke, D.J</creator><creator>Sturgill, T.W</creator><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20061121</creationdate><title>Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast</title><author>Devasahayam, G ; Ritz, D ; Helliwell, S.B ; Burke, D.J ; Sturgill, T.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f326t-3d5ed876082e1d4b3838a4e0a686da29f89a7dbfc894742c5d5bf607ac22db4d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>adenosinetriphosphatase</topic><topic>Amino Acid Transport Systems - genetics</topic><topic>Amino Acid Transport Systems - metabolism</topic><topic>Antifungal Agents - metabolism</topic><topic>Biological Sciences</topic><topic>Ca/Mn-transpoting ATPase</topic><topic>calcium</topic><topic>Calcium-Transporting ATPases - genetics</topic><topic>Calcium-Transporting ATPases - metabolism</topic><topic>Cell growth</topic><topic>Cell membranes</topic><topic>Cell nucleus</topic><topic>DNA</topic><topic>drug resistance</topic><topic>Epistasis, Genetic</topic><topic>Gene expression regulation</topic><topic>Gene Expression Regulation, Fungal</topic><topic>Genes</topic><topic>Genetics</topic><topic>Golgi apparatus</topic><topic>Golgi Apparatus - enzymology</topic><topic>Kinases</topic><topic>manganese</topic><topic>Molecular Chaperones - genetics</topic><topic>Molecular Chaperones - metabolism</topic><topic>mutants</topic><topic>Nitrogen</topic><topic>Phenotypes</topic><topic>Physiological regulation</topic><topic>Plasmids</topic><topic>PMR1 gene</topic><topic>protein kinases</topic><topic>Protein Kinases - genetics</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Serine-Threonine Kinases</topic><topic>protein transport</topic><topic>rapamycin resistance</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Signal Transduction - physiology</topic><topic>Sirolimus - metabolism</topic><topic>target of rapamycin kinase</topic><topic>Transcription Factors - metabolism</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Devasahayam, G</creatorcontrib><creatorcontrib>Ritz, D</creatorcontrib><creatorcontrib>Helliwell, S.B</creatorcontrib><creatorcontrib>Burke, D.J</creatorcontrib><creatorcontrib>Sturgill, T.W</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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>Devasahayam, G</au><au>Ritz, D</au><au>Helliwell, S.B</au><au>Burke, D.J</au><au>Sturgill, T.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2006-11-21</date><risdate>2006</risdate><volume>103</volume><issue>47</issue><spage>17840</spage><epage>17845</epage><pages>17840-17845</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The rapamycin·FKBP12 complex inhibits target of rapamycin (TOR) kinase in TORC1. We screened the yeast nonessential gene deletion collection to identify mutants that conferred rapamycin resistance, and we identified PMR1, encoding the Golgi Ca2+/Mn2+-ATPase. Deleting PMR1 in two genetic backgrounds confers rapamycin resistance. Epistasis analyses show that Pmr1 functions upstream from Npr1 and Gln-3 in opposition to Lst8, a regulator of TOR. Npr1 kinase is largely cytoplasmic, and a portion localizes to the Golgi where amino acid permeases are modified and sorted. Nuclear translocation of Gln-3 and Gln-3 reporter activity in pmr1 cells are impaired, but expression of functional Gap1 in the plasma membrane of a pmr1 strain in response to nitrogen limitation is enhanced. These two phenotypes suggest up-regulation of Npr1 function in the absence of Pmr1. Together, our results establish that Pmr1-dependent Ca2+ and/or Mn2+ ion homeostasis is necessary for TOR signaling.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>17095607</pmid><doi>10.1073/pnas.0604303103</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | adenosinetriphosphatase Amino Acid Transport Systems - genetics Amino Acid Transport Systems - metabolism Antifungal Agents - metabolism Biological Sciences Ca/Mn-transpoting ATPase calcium Calcium-Transporting ATPases - genetics Calcium-Transporting ATPases - metabolism Cell growth Cell membranes Cell nucleus DNA drug resistance Epistasis, Genetic Gene expression regulation Gene Expression Regulation, Fungal Genes Genetics Golgi apparatus Golgi Apparatus - enzymology Kinases manganese Molecular Chaperones - genetics Molecular Chaperones - metabolism mutants Nitrogen Phenotypes Physiological regulation Plasmids PMR1 gene protein kinases Protein Kinases - genetics Protein Kinases - metabolism Protein Serine-Threonine Kinases protein transport rapamycin resistance Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Signal Transduction - physiology Sirolimus - metabolism target of rapamycin kinase Transcription Factors - metabolism Yeast Yeasts |
| title | Pmr1, a Golgi Ca2+/Mn2+-ATPase, is a regulator of the target of rapamycin (TOR) signaling pathway in yeast |
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