Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1
Coligation of paired immunoglobulin-like receptor B (PIR-B) with B cell antigen receptor (BCR) blocks antigen-induced B cell activation. This inhibition is mediated in part by recruitment of SHP-1 and SHP-2 to the phosphorylated ITIMs in the cytoplasmic domain of PIR-B; however the molecular target(...
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| Veröffentlicht in: | Oncogene 1999-04, Vol.18 (14), p.2291-2297 |
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| creator | MAEDA, A SCHARENBERG, A. M TSUKADA, S BOLEN, J. B KINET, J.-P KUROSAKI, T |
| description | Coligation of paired immunoglobulin-like receptor B (PIR-B) with B cell antigen receptor (BCR) blocks antigen-induced B cell activation. This inhibition is mediated in part by recruitment of SHP-1 and SHP-2 to the phosphorylated ITIMs in the cytoplasmic domain of PIR-B; however the molecular target(s) of these phosphatases remain elusive. Here we show that PIR-B ligation inhibits the BCR-induced tyrosine phosphorylation of Igalpha/Igbeta, Syk, Btk and phospholipase C (PLC)-gamma2. Overexpression of a catalytically inactive form of SHP-1 prevents the PIR-B-mediated inhibition of tyrosine phosphorylation of Syk, Btk, and PLC-gamma2. Dephosphorylation of Syk and Btk mediated by SHP-1 leads to a decrease of their kinase activity, which in turn inhibits tyrosine phosphorylation of PLC-gamma2. Furthermore, we define a requirement for Lyn in mediating tyrosine phosphorylation of PIR-B. Based on these results, we propose a model of PIR-B-mediated inhibitory signaling in which coligation of PIR-B and BCR results in phosphorylation of ITIMs by Lyn, subsequent recruitment of SHP-1, and a resulting inhibition of the BCR-induced inositol 1,4,5-trisphosphate generation by dephosphorylation of Syk and Btk. |
| doi_str_mv | 10.1038/sj.onc.1202552 |
| format | Article |
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M ; TSUKADA, S ; BOLEN, J. B ; KINET, J.-P ; KUROSAKI, T</creator><creatorcontrib>MAEDA, A ; SCHARENBERG, A. M ; TSUKADA, S ; BOLEN, J. B ; KINET, J.-P ; KUROSAKI, T</creatorcontrib><description>Coligation of paired immunoglobulin-like receptor B (PIR-B) with B cell antigen receptor (BCR) blocks antigen-induced B cell activation. This inhibition is mediated in part by recruitment of SHP-1 and SHP-2 to the phosphorylated ITIMs in the cytoplasmic domain of PIR-B; however the molecular target(s) of these phosphatases remain elusive. Here we show that PIR-B ligation inhibits the BCR-induced tyrosine phosphorylation of Igalpha/Igbeta, Syk, Btk and phospholipase C (PLC)-gamma2. Overexpression of a catalytically inactive form of SHP-1 prevents the PIR-B-mediated inhibition of tyrosine phosphorylation of Syk, Btk, and PLC-gamma2. Dephosphorylation of Syk and Btk mediated by SHP-1 leads to a decrease of their kinase activity, which in turn inhibits tyrosine phosphorylation of PLC-gamma2. Furthermore, we define a requirement for Lyn in mediating tyrosine phosphorylation of PIR-B. Based on these results, we propose a model of PIR-B-mediated inhibitory signaling in which coligation of PIR-B and BCR results in phosphorylation of ITIMs by Lyn, subsequent recruitment of SHP-1, and a resulting inhibition of the BCR-induced inositol 1,4,5-trisphosphate generation by dephosphorylation of Syk and Btk.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1202552</identifier><identifier>PMID: 10327049</identifier><language>eng</language><publisher>Basingstoke: Nature Publishing</publisher><subject>Animals ; Antigens ; B-cell receptor ; Biological and medical sciences ; Bruton's tyrosine kinase ; Calcium Signaling - physiology ; Cell activation ; Cell Line ; Cell physiology ; Dephosphorylation ; Enzyme Activation ; Enzyme Precursors - metabolism ; Fundamental and applied biological sciences. Psychology ; Immunoglobulins ; Inositol 1,4,5-trisphosphate receptors ; Inositol Phosphates - metabolism ; Intracellular Signaling Peptides and Proteins ; Isoenzymes - antagonists & inhibitors ; Kinases ; Mice ; Models, Biological ; Molecular and cellular biology ; Phospholipase C ; Phospholipase C gamma ; Phosphorylation ; Protein Processing, Post-Translational - physiology ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases - physiology ; Protein-Tyrosine Kinases - metabolism ; Receptors, Antigen, B-Cell - immunology ; Receptors, IgG - genetics ; Receptors, Immunologic - genetics ; Receptors, Immunologic - physiology ; Recombinant Fusion Proteins - physiology ; SHP-1 protein ; SHP-2 protein ; Signal transduction ; src-Family Kinases - metabolism ; Syk Kinase ; Syk protein ; Transfection ; Type C Phospholipases - antagonists & inhibitors</subject><ispartof>Oncogene, 1999-04, Vol.18 (14), p.2291-2297</ispartof><rights>1999 INIST-CNRS</rights><rights>Macmillan Publishers Limited 1999.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c485t-c4a265fb8a66299f4b5669832b7750a1ea59308ef46a4af301aa4bf791d049c03</citedby><cites>FETCH-LOGICAL-c485t-c4a265fb8a66299f4b5669832b7750a1ea59308ef46a4af301aa4bf791d049c03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1771802$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10327049$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MAEDA, A</creatorcontrib><creatorcontrib>SCHARENBERG, A. M</creatorcontrib><creatorcontrib>TSUKADA, S</creatorcontrib><creatorcontrib>BOLEN, J. B</creatorcontrib><creatorcontrib>KINET, J.-P</creatorcontrib><creatorcontrib>KUROSAKI, T</creatorcontrib><title>Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1</title><title>Oncogene</title><addtitle>Oncogene</addtitle><description>Coligation of paired immunoglobulin-like receptor B (PIR-B) with B cell antigen receptor (BCR) blocks antigen-induced B cell activation. This inhibition is mediated in part by recruitment of SHP-1 and SHP-2 to the phosphorylated ITIMs in the cytoplasmic domain of PIR-B; however the molecular target(s) of these phosphatases remain elusive. Here we show that PIR-B ligation inhibits the BCR-induced tyrosine phosphorylation of Igalpha/Igbeta, Syk, Btk and phospholipase C (PLC)-gamma2. Overexpression of a catalytically inactive form of SHP-1 prevents the PIR-B-mediated inhibition of tyrosine phosphorylation of Syk, Btk, and PLC-gamma2. Dephosphorylation of Syk and Btk mediated by SHP-1 leads to a decrease of their kinase activity, which in turn inhibits tyrosine phosphorylation of PLC-gamma2. Furthermore, we define a requirement for Lyn in mediating tyrosine phosphorylation of PIR-B. Based on these results, we propose a model of PIR-B-mediated inhibitory signaling in which coligation of PIR-B and BCR results in phosphorylation of ITIMs by Lyn, subsequent recruitment of SHP-1, and a resulting inhibition of the BCR-induced inositol 1,4,5-trisphosphate generation by dephosphorylation of Syk and Btk.</description><subject>Animals</subject><subject>Antigens</subject><subject>B-cell receptor</subject><subject>Biological and medical sciences</subject><subject>Bruton's tyrosine kinase</subject><subject>Calcium Signaling - physiology</subject><subject>Cell activation</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Dephosphorylation</subject><subject>Enzyme Activation</subject><subject>Enzyme Precursors - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunoglobulins</subject><subject>Inositol 1,4,5-trisphosphate receptors</subject><subject>Inositol Phosphates - metabolism</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Isoenzymes - antagonists & inhibitors</subject><subject>Kinases</subject><subject>Mice</subject><subject>Models, Biological</subject><subject>Molecular and cellular biology</subject><subject>Phospholipase C</subject><subject>Phospholipase C gamma</subject><subject>Phosphorylation</subject><subject>Protein Processing, Post-Translational - physiology</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 11</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 6</subject><subject>Protein Tyrosine Phosphatases - physiology</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Receptors, Antigen, B-Cell - immunology</subject><subject>Receptors, IgG - genetics</subject><subject>Receptors, Immunologic - genetics</subject><subject>Receptors, Immunologic - physiology</subject><subject>Recombinant Fusion Proteins - physiology</subject><subject>SHP-1 protein</subject><subject>SHP-2 protein</subject><subject>Signal transduction</subject><subject>src-Family Kinases - metabolism</subject><subject>Syk Kinase</subject><subject>Syk protein</subject><subject>Transfection</subject><subject>Type C Phospholipases - antagonists & inhibitors</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c9rFDEUB_AgFrtWrx4loIgeZs3vTI7uorZQ6NLqOWQyiWZ3JtkmM8L-903ZBcVLL-9dPt8Hjy8AbzBaYkTbz2W7TNEuMUGEc_IMLDCTouFcsedggRRHjSKUnIOXpWwRQlIh8gKc1yiRiKkFcBsTsuthGMc5pl9D6uYhxGYIOwezs24_pQxX8OPm6rZZfYIh_g5dmApcrW-bEPvZ1qyxU_hjppAiTB7eHXbQxB6uph3sDvDuctPgV-DMm6G416d9AX5--_pjfdlc33y_Wn-5bixr-VSnIYL7rjVCEKU867gQqqWkk5Ijg53hiqLWeSYMM54ibAzrvFS4r89YRC_Ah-PdfU73syuTHkOxbhhMdGkuWijJCRNPQywJVy1nFb77D27TnGN9QhPBMEUUi0e1PCqbUynZeb3PYTT5oDHSjz3pstW1J33qqQbens7O3ej6f_ixmAren4Ap1gw-m2hD-eukxC0i9AGDZphS</recordid><startdate>19990408</startdate><enddate>19990408</enddate><creator>MAEDA, A</creator><creator>SCHARENBERG, A. 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M</au><au>TSUKADA, S</au><au>BOLEN, J. B</au><au>KINET, J.-P</au><au>KUROSAKI, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1</atitle><jtitle>Oncogene</jtitle><addtitle>Oncogene</addtitle><date>1999-04-08</date><risdate>1999</risdate><volume>18</volume><issue>14</issue><spage>2291</spage><epage>2297</epage><pages>2291-2297</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>Coligation of paired immunoglobulin-like receptor B (PIR-B) with B cell antigen receptor (BCR) blocks antigen-induced B cell activation. This inhibition is mediated in part by recruitment of SHP-1 and SHP-2 to the phosphorylated ITIMs in the cytoplasmic domain of PIR-B; however the molecular target(s) of these phosphatases remain elusive. Here we show that PIR-B ligation inhibits the BCR-induced tyrosine phosphorylation of Igalpha/Igbeta, Syk, Btk and phospholipase C (PLC)-gamma2. Overexpression of a catalytically inactive form of SHP-1 prevents the PIR-B-mediated inhibition of tyrosine phosphorylation of Syk, Btk, and PLC-gamma2. Dephosphorylation of Syk and Btk mediated by SHP-1 leads to a decrease of their kinase activity, which in turn inhibits tyrosine phosphorylation of PLC-gamma2. Furthermore, we define a requirement for Lyn in mediating tyrosine phosphorylation of PIR-B. Based on these results, we propose a model of PIR-B-mediated inhibitory signaling in which coligation of PIR-B and BCR results in phosphorylation of ITIMs by Lyn, subsequent recruitment of SHP-1, and a resulting inhibition of the BCR-induced inositol 1,4,5-trisphosphate generation by dephosphorylation of Syk and Btk.</abstract><cop>Basingstoke</cop><pub>Nature Publishing</pub><pmid>10327049</pmid><doi>10.1038/sj.onc.1202552</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Oncogene, 1999-04, Vol.18 (14), p.2291-2297 |
| issn | 0950-9232 1476-5594 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Antigens B-cell receptor Biological and medical sciences Bruton's tyrosine kinase Calcium Signaling - physiology Cell activation Cell Line Cell physiology Dephosphorylation Enzyme Activation Enzyme Precursors - metabolism Fundamental and applied biological sciences. Psychology Immunoglobulins Inositol 1,4,5-trisphosphate receptors Inositol Phosphates - metabolism Intracellular Signaling Peptides and Proteins Isoenzymes - antagonists & inhibitors Kinases Mice Models, Biological Molecular and cellular biology Phospholipase C Phospholipase C gamma Phosphorylation Protein Processing, Post-Translational - physiology Protein Tyrosine Phosphatase, Non-Receptor Type 11 Protein Tyrosine Phosphatase, Non-Receptor Type 6 Protein Tyrosine Phosphatases - physiology Protein-Tyrosine Kinases - metabolism Receptors, Antigen, B-Cell - immunology Receptors, IgG - genetics Receptors, Immunologic - genetics Receptors, Immunologic - physiology Recombinant Fusion Proteins - physiology SHP-1 protein SHP-2 protein Signal transduction src-Family Kinases - metabolism Syk Kinase Syk protein Transfection Type C Phospholipases - antagonists & inhibitors |
| title | Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1 |
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