Sphingosine 1-Phosphate Stimulates Tyrosine Phosphorylation of Crk
The proto-oncogene molecule c-Crk plays a role in growth factor-induced activation of Ras. Sphingosine 1-phosphate (SPP), a metabolite of cellular sphingolipids, has previously been shown to play a role in growth factor receptor signaling (Olivera, A., and Spiegel, S. (1993) Nature 365, 557–560). SP...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-06, Vol.272 (26), p.16211-16215 |
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| container_title | The Journal of biological chemistry |
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| creator | Blakesley, Vicky A. Beitner-Johnson, Dana Van Brocklyn, James R. Rani, Sheela Shen-Orr, Zila Stannard, Bethel S. Spiegel, Sarah LeRoith, Derek |
| description | The proto-oncogene molecule c-Crk plays a role in growth factor-induced activation of Ras. Sphingosine 1-phosphate (SPP), a metabolite of cellular sphingolipids, has previously been shown to play a role in growth factor receptor signaling (Olivera, A., and Spiegel, S. (1993) Nature 365, 557–560). SPP was found to strongly induce tyrosine phosphorylation of Crk, but not Shc, in NIH-3T3 parental, insulin-like growth factor-I receptor-overexpressing and Crk-overexpressing (3T3-Crk) fibroblasts. Sphingosine, a metabolic precursor of SPP, also produced a slight increase in tyrosine phosphorylation of Crk. In contrast, other sphingolipid metabolites including ceramide did not alter Crk tyrosine phosphorylation. Furthermore, Crk enhanced SPP-induced mitogenesis, as measured by SPP-stimulated [3H]thymidine incorporation in a manner proportional to the level of Crk expression in 3T3-Crk cells. This stimulation appears to be Ras-dependent, whereas SPP stimulation of MAP kinase activity is Ras-independent. These data indicate that SPP activates a tyrosine kinase that phosphorylates Crk and that Crk is a positive effector of SPP-induced mitogenesis. |
| doi_str_mv | 10.1074/jbc.272.26.16211 |
| format | Article |
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Sphingosine 1-phosphate (SPP), a metabolite of cellular sphingolipids, has previously been shown to play a role in growth factor receptor signaling (Olivera, A., and Spiegel, S. (1993) Nature 365, 557–560). SPP was found to strongly induce tyrosine phosphorylation of Crk, but not Shc, in NIH-3T3 parental, insulin-like growth factor-I receptor-overexpressing and Crk-overexpressing (3T3-Crk) fibroblasts. Sphingosine, a metabolic precursor of SPP, also produced a slight increase in tyrosine phosphorylation of Crk. In contrast, other sphingolipid metabolites including ceramide did not alter Crk tyrosine phosphorylation. Furthermore, Crk enhanced SPP-induced mitogenesis, as measured by SPP-stimulated [3H]thymidine incorporation in a manner proportional to the level of Crk expression in 3T3-Crk cells. This stimulation appears to be Ras-dependent, whereas SPP stimulation of MAP kinase activity is Ras-independent. These data indicate that SPP activates a tyrosine kinase that phosphorylates Crk and that Crk is a positive effector of SPP-induced mitogenesis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.272.26.16211</identifier><identifier>PMID: 9195921</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3T3 Cells ; Adaptor Proteins, Signal Transducing ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; GRB2 Adaptor Protein ; Lysophospholipids ; Mice ; Phosphorylation ; Proteins - metabolism ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-crk ; Sphingosine - analogs & derivatives ; Sphingosine - pharmacology ; src Homology Domains ; Tyrosine - metabolism</subject><ispartof>The Journal of biological chemistry, 1997-06, Vol.272 (26), p.16211-16215</ispartof><rights>1997 © 1997 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-6fbd9ba78b473082cab70a2a832545c75ff1ae299c27d5bcb8395c5640027a103</citedby><cites>FETCH-LOGICAL-c447t-6fbd9ba78b473082cab70a2a832545c75ff1ae299c27d5bcb8395c5640027a103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9195921$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blakesley, Vicky A.</creatorcontrib><creatorcontrib>Beitner-Johnson, Dana</creatorcontrib><creatorcontrib>Van Brocklyn, James R.</creatorcontrib><creatorcontrib>Rani, Sheela</creatorcontrib><creatorcontrib>Shen-Orr, Zila</creatorcontrib><creatorcontrib>Stannard, Bethel S.</creatorcontrib><creatorcontrib>Spiegel, Sarah</creatorcontrib><creatorcontrib>LeRoith, Derek</creatorcontrib><title>Sphingosine 1-Phosphate Stimulates Tyrosine Phosphorylation of Crk</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The proto-oncogene molecule c-Crk plays a role in growth factor-induced activation of Ras. Sphingosine 1-phosphate (SPP), a metabolite of cellular sphingolipids, has previously been shown to play a role in growth factor receptor signaling (Olivera, A., and Spiegel, S. (1993) Nature 365, 557–560). SPP was found to strongly induce tyrosine phosphorylation of Crk, but not Shc, in NIH-3T3 parental, insulin-like growth factor-I receptor-overexpressing and Crk-overexpressing (3T3-Crk) fibroblasts. Sphingosine, a metabolic precursor of SPP, also produced a slight increase in tyrosine phosphorylation of Crk. In contrast, other sphingolipid metabolites including ceramide did not alter Crk tyrosine phosphorylation. Furthermore, Crk enhanced SPP-induced mitogenesis, as measured by SPP-stimulated [3H]thymidine incorporation in a manner proportional to the level of Crk expression in 3T3-Crk cells. This stimulation appears to be Ras-dependent, whereas SPP stimulation of MAP kinase activity is Ras-independent. These data indicate that SPP activates a tyrosine kinase that phosphorylates Crk and that Crk is a positive effector of SPP-induced mitogenesis.</description><subject>3T3 Cells</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>GRB2 Adaptor Protein</subject><subject>Lysophospholipids</subject><subject>Mice</subject><subject>Phosphorylation</subject><subject>Proteins - metabolism</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-crk</subject><subject>Sphingosine - analogs & derivatives</subject><subject>Sphingosine - pharmacology</subject><subject>src Homology Domains</subject><subject>Tyrosine - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtLwzAcx4Mocz7uXoQexFtnnk3jTYcvEBRU8BaSNF2jazOTTtl_b7TDgyDmkpDvg9_vA8ABghMEOT150WaCOZ7gYoIKjNAGGCNYkpww9LwJxhBilAvMym2wE-MLTIcKNAIjgQQTGI3B-cOicd3MR9fZDOX3jY-LRvU2e-hdu5ynV8weV2HQB9WHVfp3vst8nU3D6x7YqtU82v31vQueLi8ep9f57d3VzfTsNjeU8j4val0JrXipKSewxEZpDhVWJcGMMsNZXSNlsRAG84ppo0simGEFTUtwhSDZBcdD7yL4t6WNvWxdNHY-V531yyi5SEQoJf8aUQEJJoImIxyMJi0Yg63lIrhWhZVEUH7xlYmvTHwlLuQ33xQ5XHcvdWurn8AaaNKPBr1xs-bDBSu186ax7e-a08FmE7B3Z4OMxtnO2CpFTC8r7_6e4RNf4ZTn</recordid><startdate>19970627</startdate><enddate>19970627</enddate><creator>Blakesley, Vicky A.</creator><creator>Beitner-Johnson, Dana</creator><creator>Van Brocklyn, James R.</creator><creator>Rani, Sheela</creator><creator>Shen-Orr, Zila</creator><creator>Stannard, Bethel S.</creator><creator>Spiegel, Sarah</creator><creator>LeRoith, Derek</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TO</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19970627</creationdate><title>Sphingosine 1-Phosphate Stimulates Tyrosine Phosphorylation of Crk</title><author>Blakesley, Vicky A. ; Beitner-Johnson, Dana ; Van Brocklyn, James R. ; Rani, Sheela ; Shen-Orr, Zila ; Stannard, Bethel S. ; Spiegel, Sarah ; LeRoith, Derek</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-6fbd9ba78b473082cab70a2a832545c75ff1ae299c27d5bcb8395c5640027a103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>3T3 Cells</topic><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>GRB2 Adaptor Protein</topic><topic>Lysophospholipids</topic><topic>Mice</topic><topic>Phosphorylation</topic><topic>Proteins - metabolism</topic><topic>Proto-Oncogene Proteins - metabolism</topic><topic>Proto-Oncogene Proteins c-crk</topic><topic>Sphingosine - analogs & derivatives</topic><topic>Sphingosine - pharmacology</topic><topic>src Homology Domains</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blakesley, Vicky A.</creatorcontrib><creatorcontrib>Beitner-Johnson, Dana</creatorcontrib><creatorcontrib>Van Brocklyn, James R.</creatorcontrib><creatorcontrib>Rani, Sheela</creatorcontrib><creatorcontrib>Shen-Orr, Zila</creatorcontrib><creatorcontrib>Stannard, Bethel S.</creatorcontrib><creatorcontrib>Spiegel, Sarah</creatorcontrib><creatorcontrib>LeRoith, Derek</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blakesley, Vicky A.</au><au>Beitner-Johnson, Dana</au><au>Van Brocklyn, James R.</au><au>Rani, Sheela</au><au>Shen-Orr, Zila</au><au>Stannard, Bethel S.</au><au>Spiegel, Sarah</au><au>LeRoith, Derek</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sphingosine 1-Phosphate Stimulates Tyrosine Phosphorylation of Crk</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1997-06-27</date><risdate>1997</risdate><volume>272</volume><issue>26</issue><spage>16211</spage><epage>16215</epage><pages>16211-16215</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The proto-oncogene molecule c-Crk plays a role in growth factor-induced activation of Ras. Sphingosine 1-phosphate (SPP), a metabolite of cellular sphingolipids, has previously been shown to play a role in growth factor receptor signaling (Olivera, A., and Spiegel, S. (1993) Nature 365, 557–560). SPP was found to strongly induce tyrosine phosphorylation of Crk, but not Shc, in NIH-3T3 parental, insulin-like growth factor-I receptor-overexpressing and Crk-overexpressing (3T3-Crk) fibroblasts. Sphingosine, a metabolic precursor of SPP, also produced a slight increase in tyrosine phosphorylation of Crk. In contrast, other sphingolipid metabolites including ceramide did not alter Crk tyrosine phosphorylation. Furthermore, Crk enhanced SPP-induced mitogenesis, as measured by SPP-stimulated [3H]thymidine incorporation in a manner proportional to the level of Crk expression in 3T3-Crk cells. This stimulation appears to be Ras-dependent, whereas SPP stimulation of MAP kinase activity is Ras-independent. 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| language | eng |
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| subjects | 3T3 Cells Adaptor Proteins, Signal Transducing Animals Calcium-Calmodulin-Dependent Protein Kinases - metabolism GRB2 Adaptor Protein Lysophospholipids Mice Phosphorylation Proteins - metabolism Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-crk Sphingosine - analogs & derivatives Sphingosine - pharmacology src Homology Domains Tyrosine - metabolism |
| title | Sphingosine 1-Phosphate Stimulates Tyrosine Phosphorylation of Crk |
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