Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol
Stimulation of the interleukin-2 (IL-2) receptor results in phosphorylation and activation of cytosolic Raf-1 serine/threonine kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75) in T-cell blasts. Following stimulation with IL-2,...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-08, Vol.267 (22), p.15281-15284 |
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| container_end_page | 15284 |
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| container_issue | 22 |
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| container_title | The Journal of biological chemistry |
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| creator | MASLINSKI, W REMILLARD, B TSUDO, M STROM, T. B |
| description | Stimulation of the interleukin-2 (IL-2) receptor results in phosphorylation and activation of cytosolic Raf-1 serine/threonine
kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75)
in T-cell blasts. Following stimulation with IL-2, Raf-1 dissociates from the IL-2 receptor complex and translocates to the
cytosol. Genistein, a protein tyrosine kinase inhibitor, prevents the dissociation of enzymatically active Raf-1 from the
ligand-stimulated IL-2 receptor complex. These data favor a model of IL-2 receptor activation in which an IL-2-activated protein
tyrosine kinase phosphorylates the IL-2 receptor and/or receptor-bound Raf-1. Following tyrosine phosphorylation, enzymatically
active Raf-1 dissociates from the IL-2 receptor and translocates into the cytosol. |
| doi_str_mv | 10.1016/S0021-9258(19)49530-6 |
| format | Article |
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kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75)
in T-cell blasts. Following stimulation with IL-2, Raf-1 dissociates from the IL-2 receptor complex and translocates to the
cytosol. Genistein, a protein tyrosine kinase inhibitor, prevents the dissociation of enzymatically active Raf-1 from the
ligand-stimulated IL-2 receptor complex. These data favor a model of IL-2 receptor activation in which an IL-2-activated protein
tyrosine kinase phosphorylates the IL-2 receptor and/or receptor-bound Raf-1. Following tyrosine phosphorylation, enzymatically
active Raf-1 dissociates from the IL-2 receptor and translocates into the cytosol.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)49530-6</identifier><identifier>PMID: 1639773</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Biological and medical sciences ; Blotting, Western ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; Cells, Cultured ; Cytosol - metabolism ; Fundamental and applied biological sciences. Psychology ; Humans ; Interleukin-2 - metabolism ; Interleukin-2 - pharmacology ; Methionine - blood ; Miscellaneous ; Models, Biological ; Molecular and cellular biology ; Monocytes - immunology ; Monocytes - metabolism ; Protein Kinases - blood ; Protein-Tyrosine Kinases - blood ; Proto-Oncogene Proteins - blood ; Proto-Oncogene Proteins c-raf ; Receptors, Interleukin-2 - metabolism ; Recombinant Proteins - metabolism ; Recombinant Proteins - pharmacology</subject><ispartof>The Journal of biological chemistry, 1992-08, Vol.267 (22), p.15281-15284</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-1920b85df993bbb7cf4e492a429e18efedd758e47899d6ca6dcb9da6fca2c6413</citedby><cites>FETCH-LOGICAL-c440t-1920b85df993bbb7cf4e492a429e18efedd758e47899d6ca6dcb9da6fca2c6413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5506788$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1639773$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MASLINSKI, W</creatorcontrib><creatorcontrib>REMILLARD, B</creatorcontrib><creatorcontrib>TSUDO, M</creatorcontrib><creatorcontrib>STROM, T. B</creatorcontrib><title>Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Stimulation of the interleukin-2 (IL-2) receptor results in phosphorylation and activation of cytosolic Raf-1 serine/threonine
kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75)
in T-cell blasts. Following stimulation with IL-2, Raf-1 dissociates from the IL-2 receptor complex and translocates to the
cytosol. Genistein, a protein tyrosine kinase inhibitor, prevents the dissociation of enzymatically active Raf-1 from the
ligand-stimulated IL-2 receptor complex. These data favor a model of IL-2 receptor activation in which an IL-2-activated protein
tyrosine kinase phosphorylates the IL-2 receptor and/or receptor-bound Raf-1. Following tyrosine phosphorylation, enzymatically
active Raf-1 dissociates from the IL-2 receptor and translocates into the cytosol.</description><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Membrane - metabolism</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cells, Cultured</subject><subject>Cytosol - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Interleukin-2 - metabolism</subject><subject>Interleukin-2 - pharmacology</subject><subject>Methionine - blood</subject><subject>Miscellaneous</subject><subject>Models, Biological</subject><subject>Molecular and cellular biology</subject><subject>Monocytes - immunology</subject><subject>Monocytes - metabolism</subject><subject>Protein Kinases - blood</subject><subject>Protein-Tyrosine Kinases - blood</subject><subject>Proto-Oncogene Proteins - blood</subject><subject>Proto-Oncogene Proteins c-raf</subject><subject>Receptors, Interleukin-2 - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recombinant Proteins - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuLFDEUhYMoYzv6EwayEJlZRPOqVGUpg44NDS5UcBdSyY0draq0SUpp8MdP9YOZpXcTuOe7J3AOQleMvmWUqXdfKOWMaN5010zfSN0IStQTtGK0E0Q07PtTtHpAnqMXpfyky0jNLtAFU0K3rVihf-upQh5g_hUnwvH1ekP4DY6Tnx0UXPc5lTgBXlRbgHjYweRhqrhmO5UhOVtjmnAK2Loa_wDONhCGQ04jrlvABzucwcGuprzY1nRcu31NJQ0v0bNghwKvzu8l-vbxw9fbT2Tz-W59-35DnJS0EqY57bvGB61F3_etCxKk5lZyDayDAN63TQey7bT2ylnlXa-9VcFZ7pRk4hK9Ofnucvo9Q6lmjMXBMNgJ0lxMK2iruKb_BZmSWjIqFrA5gW4JqGQIZpfjaPPeMGoO9ZhjPeaQvWHaHOsxarm7On8w9yP4x6tTH4v--qzb4uwQlpRdLA9Y01DVdt0jto0_tn9jBtPH5LYwGq5aw7lhDe-YuAeLjKRj</recordid><startdate>19920805</startdate><enddate>19920805</enddate><creator>MASLINSKI, W</creator><creator>REMILLARD, B</creator><creator>TSUDO, M</creator><creator>STROM, T. 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B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-1920b85df993bbb7cf4e492a429e18efedd758e47899d6ca6dcb9da6fca2c6413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell Membrane - metabolism</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cells, Cultured</topic><topic>Cytosol - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Interleukin-2 - metabolism</topic><topic>Interleukin-2 - pharmacology</topic><topic>Methionine - blood</topic><topic>Miscellaneous</topic><topic>Models, Biological</topic><topic>Molecular and cellular biology</topic><topic>Monocytes - immunology</topic><topic>Monocytes - metabolism</topic><topic>Protein Kinases - blood</topic><topic>Protein-Tyrosine Kinases - blood</topic><topic>Proto-Oncogene Proteins - blood</topic><topic>Proto-Oncogene Proteins c-raf</topic><topic>Receptors, Interleukin-2 - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Recombinant Proteins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MASLINSKI, W</creatorcontrib><creatorcontrib>REMILLARD, B</creatorcontrib><creatorcontrib>TSUDO, M</creatorcontrib><creatorcontrib>STROM, T. 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B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-08-05</date><risdate>1992</risdate><volume>267</volume><issue>22</issue><spage>15281</spage><epage>15284</epage><pages>15281-15284</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Stimulation of the interleukin-2 (IL-2) receptor results in phosphorylation and activation of cytosolic Raf-1 serine/threonine
kinase. Herein, we report that enzymatically active Raf-1 is physically associated with the IL-2 receptor beta chain (p75)
in T-cell blasts. Following stimulation with IL-2, Raf-1 dissociates from the IL-2 receptor complex and translocates to the
cytosol. Genistein, a protein tyrosine kinase inhibitor, prevents the dissociation of enzymatically active Raf-1 from the
ligand-stimulated IL-2 receptor complex. These data favor a model of IL-2 receptor activation in which an IL-2-activated protein
tyrosine kinase phosphorylates the IL-2 receptor and/or receptor-bound Raf-1. Following tyrosine phosphorylation, enzymatically
active Raf-1 dissociates from the IL-2 receptor and translocates into the cytosol.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1639773</pmid><doi>10.1016/S0021-9258(19)49530-6</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Blotting, Western Cell Membrane - metabolism Cell receptors Cell structures and functions Cells, Cultured Cytosol - metabolism Fundamental and applied biological sciences. Psychology Humans Interleukin-2 - metabolism Interleukin-2 - pharmacology Methionine - blood Miscellaneous Models, Biological Molecular and cellular biology Monocytes - immunology Monocytes - metabolism Protein Kinases - blood Protein-Tyrosine Kinases - blood Proto-Oncogene Proteins - blood Proto-Oncogene Proteins c-raf Receptors, Interleukin-2 - metabolism Recombinant Proteins - metabolism Recombinant Proteins - pharmacology |
| title | Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol |
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