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The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation
The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been ad...
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Published in: | The EMBO journal 2001-12, Vol.20 (24), p.7085-7095 |
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container_title | The EMBO journal |
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creator | Rao, Navin Ghosh, Amiya K. Ota, Satoshi Zhou, Pengcheng Reddi, Alagarsamy Lakku Hakezi, Kaoru Druker, Brian K. Wu, Jiong Band, Hamid |
description | The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been addressed, nor is it known whether these kinases are regulated via ubiquitylation during lymphocyte B‐cell receptor engagement. Here we show that B‐cell receptor stimulation in Ramos cells induces the ubiquitylation of Syk tyrosine kinase which is inhibited by a dominant‐negative mutant of Cbl. Intact tyrosine kinase‐binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for
in vitro
Syk ubiquitylation. These same domains were also essential for Cbl‐mediated negative regulation of Syk as measured using an NFAT‐luciferase reporter in a lymphoid cell. Association with Cbl did not alter the kinase activity of Syk. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl‐mediated negative regulation of cytoplasmic targets. |
doi_str_mv | 10.1093/emboj/20.24.7085 |
format | article |
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in vitro
Syk ubiquitylation. These same domains were also essential for Cbl‐mediated negative regulation of Syk as measured using an NFAT‐luciferase reporter in a lymphoid cell. Association with Cbl did not alter the kinase activity of Syk. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl‐mediated negative regulation of cytoplasmic targets.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.24.7085</identifier><identifier>PMID: 11742985</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>activation ; Cell Line ; Cysteine Endopeptidases - drug effects ; Cysteine Proteinase Inhibitors - pharmacology ; Enzyme Precursors - metabolism ; Humans ; Intracellular Signaling Peptides and Proteins ; lymphocyte ; Lymphocytes ; Multienzyme Complexes - drug effects ; Oncogene Protein v-cbl ; Proteasome Endopeptidase Complex ; Protein-Tyrosine Kinases - metabolism ; Receptors, Antigen, B-Cell - metabolism ; Recombinant Proteins - metabolism ; regulation ; Retroviridae Proteins, Oncogenic - metabolism ; Syk Kinase ; Syk protein ; tyrosine kinase ; Ubiquitin - metabolism ; ubiquitylation ; ZAP-70 protein</subject><ispartof>The EMBO journal, 2001-12, Vol.20 (24), p.7085-7095</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Dec 17, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6676-ac4d277675d2b3aa34dc92fa2a99b57add91412b4db0826aef018dca1b71874d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125791/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125791/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11742985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rao, Navin</creatorcontrib><creatorcontrib>Ghosh, Amiya K.</creatorcontrib><creatorcontrib>Ota, Satoshi</creatorcontrib><creatorcontrib>Zhou, Pengcheng</creatorcontrib><creatorcontrib>Reddi, Alagarsamy Lakku</creatorcontrib><creatorcontrib>Hakezi, Kaoru</creatorcontrib><creatorcontrib>Druker, Brian K.</creatorcontrib><creatorcontrib>Wu, Jiong</creatorcontrib><creatorcontrib>Band, Hamid</creatorcontrib><title>The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been addressed, nor is it known whether these kinases are regulated via ubiquitylation during lymphocyte B‐cell receptor engagement. Here we show that B‐cell receptor stimulation in Ramos cells induces the ubiquitylation of Syk tyrosine kinase which is inhibited by a dominant‐negative mutant of Cbl. Intact tyrosine kinase‐binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for
in vitro
Syk ubiquitylation. These same domains were also essential for Cbl‐mediated negative regulation of Syk as measured using an NFAT‐luciferase reporter in a lymphoid cell. Association with Cbl did not alter the kinase activity of Syk. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl‐mediated negative regulation of cytoplasmic targets.</description><subject>activation</subject><subject>Cell Line</subject><subject>Cysteine Endopeptidases - drug effects</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>Enzyme Precursors - metabolism</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>lymphocyte</subject><subject>Lymphocytes</subject><subject>Multienzyme Complexes - drug effects</subject><subject>Oncogene Protein v-cbl</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Receptors, Antigen, B-Cell - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>regulation</subject><subject>Retroviridae Proteins, Oncogenic - metabolism</subject><subject>Syk Kinase</subject><subject>Syk protein</subject><subject>tyrosine kinase</subject><subject>Ubiquitin - metabolism</subject><subject>ubiquitylation</subject><subject>ZAP-70 protein</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNqFkc9v0zAcxSMEYmVw5wKyOHBL569jx_GBw1rtB9MGB4YmcbGcxO3cpnZnO4z-97ik6gYS2sU-fN_n-X39suwt4DFgURzpVe0WRwSPCR1zXLFn2QhoiXOCOXuejTApIadQiYPsVQgLjDGrOLzMDgA4JaJio2x9fauRdTb3utHr6DyKG--CsRotjVVBo2-bJTIBKRSVn-uI3AxN6y5f6daoqFvU1-auN3HTqWicRf06HZO80V2H9p4hmlU_CF5nL2aqC_rN7j7Mvp-eXE_P88uvZ5-nx5d5U5a8zFVDW8J5yVlL6kKpgraNIDNFlBA146ptBVAgNW1rXJFS6RmGqm0U1BwqTtviMPs0-K77OmVttI1edXLtzUr5jXTKyL8n1tzKufspgTAuIPEfd7x3d70OUa5M2G6lrHZ9kJwUjJQVe1IIFQGCGUnCD_8IF673Nn2CBJG8OKNbER5ETWoheD3bJwYst53LP51LgiWhctt5Qt4_3vQB2JWcBGIQ3JtOb540lCdXkwvOBAVRJhYGNiTMzrV_FPr_gd4NjFWx93r_4INnPsxNiPrXfqz8Upa84EzefDmTE_rj4up8Wsmb4jfRW-YY</recordid><startdate>20011217</startdate><enddate>20011217</enddate><creator>Rao, Navin</creator><creator>Ghosh, Amiya K.</creator><creator>Ota, Satoshi</creator><creator>Zhou, Pengcheng</creator><creator>Reddi, Alagarsamy Lakku</creator><creator>Hakezi, Kaoru</creator><creator>Druker, Brian K.</creator><creator>Wu, Jiong</creator><creator>Band, Hamid</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20011217</creationdate><title>The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation</title><author>Rao, Navin ; Ghosh, Amiya K. ; Ota, Satoshi ; Zhou, Pengcheng ; Reddi, Alagarsamy Lakku ; Hakezi, Kaoru ; Druker, Brian K. ; Wu, Jiong ; Band, Hamid</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6676-ac4d277675d2b3aa34dc92fa2a99b57add91412b4db0826aef018dca1b71874d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>activation</topic><topic>Cell Line</topic><topic>Cysteine Endopeptidases - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rao, Navin</au><au>Ghosh, Amiya K.</au><au>Ota, Satoshi</au><au>Zhou, Pengcheng</au><au>Reddi, Alagarsamy Lakku</au><au>Hakezi, Kaoru</au><au>Druker, Brian K.</au><au>Wu, Jiong</au><au>Band, Hamid</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-12-17</date><risdate>2001</risdate><volume>20</volume><issue>24</issue><spage>7085</spage><epage>7095</epage><pages>7085-7095</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The negative regulator Cbl functions as a ubiquitin ligase towards activated receptor tyrosine kinases and facilitates their transport to lysosomes. Whether Cbl ubiquitin ligase activity mediates its negative regulatory effects on cytoplasmic tyrosine kinases of the Syk/ZAP‐70 family has not been addressed, nor is it known whether these kinases are regulated via ubiquitylation during lymphocyte B‐cell receptor engagement. Here we show that B‐cell receptor stimulation in Ramos cells induces the ubiquitylation of Syk tyrosine kinase which is inhibited by a dominant‐negative mutant of Cbl. Intact tyrosine kinase‐binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for
in vitro
Syk ubiquitylation. These same domains were also essential for Cbl‐mediated negative regulation of Syk as measured using an NFAT‐luciferase reporter in a lymphoid cell. Association with Cbl did not alter the kinase activity of Syk. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl‐mediated negative regulation of cytoplasmic targets.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11742985</pmid><doi>10.1093/emboj/20.24.7085</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | activation Cell Line Cysteine Endopeptidases - drug effects Cysteine Proteinase Inhibitors - pharmacology Enzyme Precursors - metabolism Humans Intracellular Signaling Peptides and Proteins lymphocyte Lymphocytes Multienzyme Complexes - drug effects Oncogene Protein v-cbl Proteasome Endopeptidase Complex Protein-Tyrosine Kinases - metabolism Receptors, Antigen, B-Cell - metabolism Recombinant Proteins - metabolism regulation Retroviridae Proteins, Oncogenic - metabolism Syk Kinase Syk protein tyrosine kinase Ubiquitin - metabolism ubiquitylation ZAP-70 protein |
title | The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation |
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