PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation
PHAS-I is a heat-stable protein (relative molecular mass $\approx$12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS...
Gespeichert in:
| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1994-10, Vol.266 (5185), p.653-656 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 656 |
|---|---|
| container_issue | 5185 |
| container_start_page | 653 |
| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 266 |
| creator | Lin, Tai-An Kong, Xianming Timothy A. J. Haystead Pause, Arnim Belsham, Graham Sonenberg, Nahum Lawrence, John C. |
| description | PHAS-I is a heat-stable protein (relative molecular mass $\approx$12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase. |
| doi_str_mv | 10.1126/science.7939721 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_76776415</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A15898455</galeid><jstor_id>2885450</jstor_id><sourcerecordid>A15898455</sourcerecordid><originalsourceid>FETCH-LOGICAL-c628t-b0118483ab7979e9cbc9fac64b035ac252b9c403aabed21ca94ae93e83f83b473</originalsourceid><addsrcrecordid>eNqN0s9v0zAUB_AIgUYZnLmA5ANCHJbNjuPYPnYVdNUKnbTC1XpxXiqP1Bmxy4__noxGnSpVovLBlr8fv4PfS5LXjJ4zlhUXwTr0Fs-l5lpm7EkyYlSLVGeUP01GlPIiVVSK58mLEO4o7TPNT5KTgY-S5c3V-DadEQgEyNz57-QS4y9ETz672K7Qp2Mb3U-IWJGbro3oPLl2HgIS8BVZduBDA9G1nsy8i-7f8WXyrIYm4KthP02-fvq4nFyl88V0NhnPU1tkKqYlZUzlikMptdSobWl1DbbIS8oF2ExkpbY55QAlVhmzoHNAzVHxWvEyl_w0eb-te9-1PzYYolm7YLFpwGO7CUYWUhY5E_-FrBCFZIXu4dkWrqBB43zdxg5s_w3YQdN6rF1_PWZCaZWLh7rpAd6vCtfOHvIf9nxPIv6OK9iEYGa3X46mi29H08vpsVRN53v07BC1bdPgCk3fyMlij19sue3aEDqszX3n1tD9MYyah1E1w6iaYfb6F2-HpmzKNVY7_5i_G3IIFpq6HzXrwo5xziQTWc_ebNldiG23izOlRC4o_wurDvZ2</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16567169</pqid></control><display><type>article</type><title>PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation</title><source>American Association for the Advancement of Science</source><source>Jstor Complete Legacy</source><source>MEDLINE</source><creator>Lin, Tai-An ; Kong, Xianming ; Timothy A. J. Haystead ; Pause, Arnim ; Belsham, Graham ; Sonenberg, Nahum ; Lawrence, John C.</creator><creatorcontrib>Lin, Tai-An ; Kong, Xianming ; Timothy A. J. Haystead ; Pause, Arnim ; Belsham, Graham ; Sonenberg, Nahum ; Lawrence, John C.</creatorcontrib><description>PHAS-I is a heat-stable protein (relative molecular mass $\approx$12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.7939721</identifier><identifier>PMID: 7939721</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>3T3 Cells ; Adipocytes ; Adipocytes - metabolism ; Animals ; Antibodies ; Antiserum ; Awards ; Biological and medical sciences ; Carrier Proteins ; Cell physiology ; Fundamental and applied biological sciences. Psychology ; Growth factors ; Homogenization ; Insulin ; Insulin - pharmacology ; Mice ; Mitogen-Activated Protein Kinase 1 ; Molecular and cellular biology ; Peptide Initiation Factors - isolation & purification ; Peptide Initiation Factors - metabolism ; Phosphoproteins - metabolism ; Phosphorylation ; Physiological aspects ; Protein Biosynthesis ; Protein synthesis ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Rats ; Recombinant Proteins - metabolism ; Resins ; Serine - metabolism ; Signal transduction ; Synthesis</subject><ispartof>Science (American Association for the Advancement of Science), 1994-10, Vol.266 (5185), p.653-656</ispartof><rights>Copyright 1994 American Association for the Advancement of Science</rights><rights>1995 INIST-CNRS</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><rights>COPYRIGHT 1994 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c628t-b0118483ab7979e9cbc9fac64b035ac252b9c403aabed21ca94ae93e83f83b473</citedby><cites>FETCH-LOGICAL-c628t-b0118483ab7979e9cbc9fac64b035ac252b9c403aabed21ca94ae93e83f83b473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2885450$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2885450$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3317152$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7939721$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lin, Tai-An</creatorcontrib><creatorcontrib>Kong, Xianming</creatorcontrib><creatorcontrib>Timothy A. J. Haystead</creatorcontrib><creatorcontrib>Pause, Arnim</creatorcontrib><creatorcontrib>Belsham, Graham</creatorcontrib><creatorcontrib>Sonenberg, Nahum</creatorcontrib><creatorcontrib>Lawrence, John C.</creatorcontrib><title>PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>PHAS-I is a heat-stable protein (relative molecular mass $\approx$12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.</description><subject>3T3 Cells</subject><subject>Adipocytes</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antiserum</subject><subject>Awards</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins</subject><subject>Cell physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Growth factors</subject><subject>Homogenization</subject><subject>Insulin</subject><subject>Insulin - pharmacology</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinase 1</subject><subject>Molecular and cellular biology</subject><subject>Peptide Initiation Factors - isolation & purification</subject><subject>Peptide Initiation Factors - metabolism</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein Biosynthesis</subject><subject>Protein synthesis</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Recombinant Proteins - metabolism</subject><subject>Resins</subject><subject>Serine - metabolism</subject><subject>Signal transduction</subject><subject>Synthesis</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0s9v0zAUB_AIgUYZnLmA5ANCHJbNjuPYPnYVdNUKnbTC1XpxXiqP1Bmxy4__noxGnSpVovLBlr8fv4PfS5LXjJ4zlhUXwTr0Fs-l5lpm7EkyYlSLVGeUP01GlPIiVVSK58mLEO4o7TPNT5KTgY-S5c3V-DadEQgEyNz57-QS4y9ETz672K7Qp2Mb3U-IWJGbro3oPLl2HgIS8BVZduBDA9G1nsy8i-7f8WXyrIYm4KthP02-fvq4nFyl88V0NhnPU1tkKqYlZUzlikMptdSobWl1DbbIS8oF2ExkpbY55QAlVhmzoHNAzVHxWvEyl_w0eb-te9-1PzYYolm7YLFpwGO7CUYWUhY5E_-FrBCFZIXu4dkWrqBB43zdxg5s_w3YQdN6rF1_PWZCaZWLh7rpAd6vCtfOHvIf9nxPIv6OK9iEYGa3X46mi29H08vpsVRN53v07BC1bdPgCk3fyMlij19sue3aEDqszX3n1tD9MYyah1E1w6iaYfb6F2-HpmzKNVY7_5i_G3IIFpq6HzXrwo5xziQTWc_ebNldiG23izOlRC4o_wurDvZ2</recordid><startdate>19941028</startdate><enddate>19941028</enddate><creator>Lin, Tai-An</creator><creator>Kong, Xianming</creator><creator>Timothy A. J. Haystead</creator><creator>Pause, Arnim</creator><creator>Belsham, Graham</creator><creator>Sonenberg, Nahum</creator><creator>Lawrence, John C.</creator><general>American Society for the Advancement of Science</general><general>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>7TM</scope><scope>7TO</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19941028</creationdate><title>PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation</title><author>Lin, Tai-An ; Kong, Xianming ; Timothy A. J. Haystead ; Pause, Arnim ; Belsham, Graham ; Sonenberg, Nahum ; Lawrence, John C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c628t-b0118483ab7979e9cbc9fac64b035ac252b9c403aabed21ca94ae93e83f83b473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>3T3 Cells</topic><topic>Adipocytes</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antiserum</topic><topic>Awards</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins</topic><topic>Cell physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Growth factors</topic><topic>Homogenization</topic><topic>Insulin</topic><topic>Insulin - pharmacology</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase 1</topic><topic>Molecular and cellular biology</topic><topic>Peptide Initiation Factors - isolation & purification</topic><topic>Peptide Initiation Factors - metabolism</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Protein Biosynthesis</topic><topic>Protein synthesis</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Rats</topic><topic>Recombinant Proteins - metabolism</topic><topic>Resins</topic><topic>Serine - metabolism</topic><topic>Signal transduction</topic><topic>Synthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Tai-An</creatorcontrib><creatorcontrib>Kong, Xianming</creatorcontrib><creatorcontrib>Timothy A. J. Haystead</creatorcontrib><creatorcontrib>Pause, Arnim</creatorcontrib><creatorcontrib>Belsham, Graham</creatorcontrib><creatorcontrib>Sonenberg, Nahum</creatorcontrib><creatorcontrib>Lawrence, John C.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - 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>Lin, Tai-An</au><au>Kong, Xianming</au><au>Timothy A. J. Haystead</au><au>Pause, Arnim</au><au>Belsham, Graham</au><au>Sonenberg, Nahum</au><au>Lawrence, John C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1994-10-28</date><risdate>1994</risdate><volume>266</volume><issue>5185</issue><spage>653</spage><epage>656</epage><pages>653-656</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>PHAS-I is a heat-stable protein (relative molecular mass $\approx$12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>7939721</pmid><doi>10.1126/science.7939721</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1994-10, Vol.266 (5185), p.653-656 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76776415 |
| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | 3T3 Cells Adipocytes Adipocytes - metabolism Animals Antibodies Antiserum Awards Biological and medical sciences Carrier Proteins Cell physiology Fundamental and applied biological sciences. Psychology Growth factors Homogenization Insulin Insulin - pharmacology Mice Mitogen-Activated Protein Kinase 1 Molecular and cellular biology Peptide Initiation Factors - isolation & purification Peptide Initiation Factors - metabolism Phosphoproteins - metabolism Phosphorylation Physiological aspects Protein Biosynthesis Protein synthesis Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases - metabolism Proteins Rats Recombinant Proteins - metabolism Resins Serine - metabolism Signal transduction Synthesis |
| title | PHAS-I as a Link Between Mitogen-Activated Protein Kinase and Translation Initiation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T23%3A13%3A39IST&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=PHAS-I%20as%20a%20Link%20Between%20Mitogen-Activated%20Protein%20Kinase%20and%20Translation%20Initiation&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Lin,%20Tai-An&rft.date=1994-10-28&rft.volume=266&rft.issue=5185&rft.spage=653&rft.epage=656&rft.pages=653-656&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.7939721&rft_dat=%3Cgale_proqu%3EA15898455%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=16567169&rft_id=info:pmid/7939721&rft_galeid=A15898455&rft_jstor_id=2885450&rfr_iscdi=true |