Ste5 RING-H2 Domain: Role in Ste4-Promoted Oligomerization for Yeast Pheromone Signaling
Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the β subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascad...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1997-10, Vol.278 (5335), p.103-106 |
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| creator | Inouye, Carla Dhillon, Namrita Thorner, Jeremy |
| description | Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the β subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Δ cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Δ cell and an ste4Δ ste5Δ double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling. |
| doi_str_mv | 10.1126/science.278.5335.103 |
| format | Article |
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Ste5 also associates with Ste4, the β subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Δ cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Δ cell and an ste4Δ ste5Δ double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.278.5335.103</identifier><identifier>PMID: 9311911</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Adaptor Proteins, Signal Transducing ; Alleles ; Amino Acid Sequence ; Binding Sites ; Biological and medical sciences ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Carrier Proteins ; Cell cycle ; Cells ; Chimeras ; Classical genetics, quantitative genetics, hybrids ; Dimerization ; Diploidy ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Genetic Complementation Test ; Genetics of eukaryotes. Biological and molecular evolution ; Glutathione Transferase - chemistry ; GTP-Binding Protein beta Subunits ; GTP-Binding Proteins - metabolism ; Heterotrimeric GTP-Binding Proteins ; Kinases ; Literary Devices ; Mathematical functions ; Mating Factor ; Molecular Sequence Data ; Mutant proteins ; Mutation ; Peptides - physiology ; Pheromones ; Pheromones - physiology ; Physiological aspects ; Plasmids ; Point Mutation ; Polymers ; Proteins ; Recombinant Fusion Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Sexual recognition (Zoology) ; Signal Transduction ; Thallophyta, bryophyta ; Transformation, Genetic ; Vegetals ; Yeast ; Yeast (Food product) ; Yeasts</subject><ispartof>Science (American Association for the Advancement of Science), 1997-10, Vol.278 (5335), p.103-106</ispartof><rights>Copyright 1997 American Association for the Advancement of Science</rights><rights>1997 INIST-CNRS</rights><rights>COPYRIGHT 1997 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Oct 3, 1997</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c840t-4c18de1db97d90de43f3953ebcd7cc74bc9320c59ae5bb1b26619baa0944d4f43</citedby><cites>FETCH-LOGICAL-c840t-4c18de1db97d90de43f3953ebcd7cc74bc9320c59ae5bb1b26619baa0944d4f43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2894516$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2894516$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,2884,2885,27924,27925,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2851151$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9311911$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Inouye, Carla</creatorcontrib><creatorcontrib>Dhillon, Namrita</creatorcontrib><creatorcontrib>Thorner, Jeremy</creatorcontrib><title>Ste5 RING-H2 Domain: Role in Ste4-Promoted Oligomerization for Yeast Pheromone Signaling</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the β subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Δ cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Δ cell and an ste4Δ ste5Δ double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Carrier Proteins</subject><subject>Cell cycle</subject><subject>Cells</subject><subject>Chimeras</subject><subject>Classical genetics, quantitative genetics, hybrids</subject><subject>Dimerization</subject><subject>Diploidy</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Genetic Complementation Test</subject><subject>Genetics of eukaryotes. 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metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sexual recognition (Zoology)</subject><subject>Signal Transduction</subject><subject>Thallophyta, bryophyta</subject><subject>Transformation, Genetic</subject><subject>Vegetals</subject><subject>Yeast</subject><subject>Yeast (Food product)</subject><subject>Yeasts</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqN0-9r1DAYB_AiypzT_2BCkaG-sGd-to3v5qm3g2M3dir6KqTp05qjbWbSA_WvN-XK3OTYjr4o9PvpN5DkiaJjjCYYk_St1wY6DROS5RNOKZ9gRB9EhxgJngiC6MPoECGaJjnK-OPoifdrhEIm6EF0ICjGAuPD6NuqBx5fzs9nyRmJP9hWme5dfGkbiE0Xh5AlF862tocyXjamti0480f1xnZxZV38HZTv44sfMKAO4pWpO9WYrn4aPapU4-HZ-D6Kvnz6-Hl6liyWs_n0dJHonKE-YRrnJeCyEFkpUAmMVlRwCoUuM60zVmhBCdJcKOBFgQuSplgUSiHBWMkqRo-il9veK2d_bsD3sjVeQ9OoDuzGy0xQJEhOA3x1N2Q042lK7q8kmGFKQ-d9EKco5yQlAb74D67txoWNGsooD-ti_A_VqgFpusr2TumhUZ4SRMKqAgX0ZgeqoQOnmnAAlQmfb_JkBw9PCa3Ru_zrWz6QHn71tdp4L-er873p8uve9P1sX5rPFndsxUi1bRqoQYZbNl3e4mzLtbPeO6jklTOtcr8lRnIYKDkOlAwDJYeBCsFwbZ6PR7cpWiivfxonKOQnY668Vk3lVKeNv2Yk5xjzgR1v2dr31t2IBeM4pX8B3XMqmg</recordid><startdate>19971003</startdate><enddate>19971003</enddate><creator>Inouye, Carla</creator><creator>Dhillon, Namrita</creator><creator>Thorner, Jeremy</creator><general>American Society for the Advancement of Science</general><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</general><scope>IQODW</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>0-V</scope><scope>3V.</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88B</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8BQ</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ALSLI</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CJNVE</scope><scope>D1I</scope><scope>DWQXO</scope><scope>F28</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>HCIFZ</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9-</scope><scope>K9.</scope><scope>KB.</scope><scope>KR7</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>L~C</scope><scope>L~D</scope><scope>M0K</scope><scope>M0P</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEDU</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19971003</creationdate><title>Ste5 RING-H2 Domain: Role in Ste4-Promoted Oligomerization for Yeast Pheromone Signaling</title><author>Inouye, Carla ; Dhillon, Namrita ; Thorner, Jeremy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c840t-4c18de1db97d90de43f3953ebcd7cc74bc9320c59ae5bb1b26619baa0944d4f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Alleles</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Carrier Proteins</topic><topic>Cell cycle</topic><topic>Cells</topic><topic>Chimeras</topic><topic>Classical genetics, quantitative genetics, hybrids</topic><topic>Dimerization</topic><topic>Diploidy</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Genetic Complementation Test</topic><topic>Genetics of eukaryotes. 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Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Inouye, Carla</au><au>Dhillon, Namrita</au><au>Thorner, Jeremy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ste5 RING-H2 Domain: Role in Ste4-Promoted Oligomerization for Yeast Pheromone Signaling</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1997-10-03</date><risdate>1997</risdate><volume>278</volume><issue>5335</issue><spage>103</spage><epage>106</epage><pages>103-106</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Ste5 is a scaffold for the mitogen-activated protein kinase (MAPK) cascade components in a yeast pheromone response pathway. Ste5 also associates with Ste4, the β subunit of a heterotrimeric guanine nucleotide-binding protein, potentially linking receptor activation to stimulation of the MAPK cascade. A RING-H2 motif at the Ste5 amino terminus is apparently essential for function because Ste5(C177S) and Ste5(C177A C180A) mutants did not rescue the mating defect of a ste5Δ cell. In vitro Ste5(C177A C180A) bound each component of the MAPK cascade, but not Ste4. Unlike wild-type Ste5, the mutant did not appear to oligomerize; however, when fused to a heterologous dimerization domain (glutathione S-transferase), the chimeric protein restored mating in an ste5Δ cell and an ste4Δ ste5Δ double mutant. Thus, the RING-H2 domain mediates Ste4-Ste5 interaction, which is a prerequisite for Ste5-Ste5 self-association and signaling.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9311911</pmid><doi>10.1126/science.278.5335.103</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1997-10, Vol.278 (5335), p.103-106 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79309283 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; American Association for the Advancement of Science |
| subjects | Adaptor Proteins, Signal Transducing Alleles Amino Acid Sequence Binding Sites Biological and medical sciences Calcium-Calmodulin-Dependent Protein Kinases - metabolism Carrier Proteins Cell cycle Cells Chimeras Classical genetics, quantitative genetics, hybrids Dimerization Diploidy Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Genetic Complementation Test Genetics of eukaryotes. Biological and molecular evolution Glutathione Transferase - chemistry GTP-Binding Protein beta Subunits GTP-Binding Proteins - metabolism Heterotrimeric GTP-Binding Proteins Kinases Literary Devices Mathematical functions Mating Factor Molecular Sequence Data Mutant proteins Mutation Peptides - physiology Pheromones Pheromones - physiology Physiological aspects Plasmids Point Mutation Polymers Proteins Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Sexual recognition (Zoology) Signal Transduction Thallophyta, bryophyta Transformation, Genetic Vegetals Yeast Yeast (Food product) Yeasts |
| title | Ste5 RING-H2 Domain: Role in Ste4-Promoted Oligomerization for Yeast Pheromone Signaling |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-02T12%3A14%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ste5%20RING-H2%20Domain:%20Role%20in%20Ste4-Promoted%20Oligomerization%20for%20Yeast%20Pheromone%20Signaling&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Inouye,%20Carla&rft.date=1997-10-03&rft.volume=278&rft.issue=5335&rft.spage=103&rft.epage=106&rft.pages=103-106&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.278.5335.103&rft_dat=%3Cgale_proqu%3EA20221490%3C/gale_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=213575611&rft_id=info:pmid/9311911&rft_galeid=A20221490&rft_jstor_id=2894516&rfr_iscdi=true |