Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals
Tec family non‐receptor tyrosine kinases have been implicated in signal transduction events initiated by cell surface receptors from a broad range of cell types, including an essential role in B‐cell development. A unique feature of several Tec members among known tyrosine kinases is the presence of...
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| Veröffentlicht in: | The EMBO journal 1998-04, Vol.17 (7), p.1961-1972 |
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| container_end_page | 1972 |
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| container_issue | 7 |
| container_start_page | 1961 |
| container_title | The EMBO journal |
| container_volume | 17 |
| creator | Scharenberg, Andrew M. El-Hillal, Ousama Fruman, David A. Beitz, Laurie O. Li, Zuomei Lin, Siqi Gout, Ivan Cantley, Lewis C. Rawlings, David J. Kinet, Jean-Pierre |
| description | Tec family non‐receptor tyrosine kinases have been implicated in signal transduction events initiated by cell surface receptors from a broad range of cell types, including an essential role in B‐cell development. A unique feature of several Tec members among known tyrosine kinases is the presence of an N‐terminal pleckstrin homology (PH) domain. We directly demonstrate that phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns‐3,4,5‐P3) interacting with the PH domain acts as an upstream activation signal for Tec kinases, resulting in Tec kinase‐dependent phospholipase Cγ (PLCγ) tyrosine phosphorylation and inositol trisphosphate production. In addition, we show that this pathway is blocked when an SH2‐containing inositol phosphatase (SHIP)‐dependent inhibitory receptor is engaged. Together, our results suggest a general mechanism whereby PtdIns‐3,4,5‐P3 regulates receptor‐dependent calcium signals through the function of Tec kinases. |
| doi_str_mv | 10.1093/emboj/17.7.1961 |
| format | Article |
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A unique feature of several Tec members among known tyrosine kinases is the presence of an N‐terminal pleckstrin homology (PH) domain. We directly demonstrate that phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns‐3,4,5‐P3) interacting with the PH domain acts as an upstream activation signal for Tec kinases, resulting in Tec kinase‐dependent phospholipase Cγ (PLCγ) tyrosine phosphorylation and inositol trisphosphate production. In addition, we show that this pathway is blocked when an SH2‐containing inositol phosphatase (SHIP)‐dependent inhibitory receptor is engaged. Together, our results suggest a general mechanism whereby PtdIns‐3,4,5‐P3 regulates receptor‐dependent calcium signals through the function of Tec kinases.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/17.7.1961</identifier><identifier>PMID: 9524119</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; B-cells ; Blood Proteins - genetics ; Calcium - physiology ; Cell Line, Transformed ; Enzyme Activation ; Enzyme Inhibitors - pharmacology ; Fibroblasts ; Inositol Phosphates - biosynthesis ; inositol trisphosphate ; Isoenzymes - metabolism ; Mutation ; Phosphatidylinositol 3-Kinases - antagonists & inhibitors ; Phosphatidylinositol 3-Kinases - physiology ; Phosphatidylinositol Phosphates - genetics ; Phosphatidylinositol Phosphates - physiology ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases ; phospholipase C ; Phospholipase C gamma ; Phosphoproteins ; Phosphoric Monoester Hydrolases - physiology ; Phosphorylation ; Protein-Tyrosine Kinases - genetics ; Protein-Tyrosine Kinases - metabolism ; Protein-Tyrosine Kinases - physiology ; Rats ; receptor ; Receptors, Antigen, B-Cell - metabolism ; Receptors, IgG - physiology ; Sequence Homology, Amino Acid ; Signal Transduction - physiology ; Type C Phospholipases - metabolism ; Tyrosine - metabolism ; tyrosine kinases</subject><ispartof>The EMBO journal, 1998-04, Vol.17 (7), p.1961-1972</ispartof><rights>Copyright © 1998 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5729-abb7e5c8d8d1ea3a82c958125ac1b2d8e1e1f01c3ae1ee9aef321d13842778213</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/PMC1170542/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170542/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9524119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scharenberg, Andrew M.</creatorcontrib><creatorcontrib>El-Hillal, Ousama</creatorcontrib><creatorcontrib>Fruman, David A.</creatorcontrib><creatorcontrib>Beitz, Laurie O.</creatorcontrib><creatorcontrib>Li, Zuomei</creatorcontrib><creatorcontrib>Lin, Siqi</creatorcontrib><creatorcontrib>Gout, Ivan</creatorcontrib><creatorcontrib>Cantley, Lewis C.</creatorcontrib><creatorcontrib>Rawlings, David J.</creatorcontrib><creatorcontrib>Kinet, Jean-Pierre</creatorcontrib><title>Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>Tec family non‐receptor tyrosine kinases have been implicated in signal transduction events initiated by cell surface receptors from a broad range of cell types, including an essential role in B‐cell development. A unique feature of several Tec members among known tyrosine kinases is the presence of an N‐terminal pleckstrin homology (PH) domain. We directly demonstrate that phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns‐3,4,5‐P3) interacting with the PH domain acts as an upstream activation signal for Tec kinases, resulting in Tec kinase‐dependent phospholipase Cγ (PLCγ) tyrosine phosphorylation and inositol trisphosphate production. In addition, we show that this pathway is blocked when an SH2‐containing inositol phosphatase (SHIP)‐dependent inhibitory receptor is engaged. Together, our results suggest a general mechanism whereby PtdIns‐3,4,5‐P3 regulates receptor‐dependent calcium signals through the function of Tec kinases.</description><subject>Animals</subject><subject>B-cells</subject><subject>Blood Proteins - genetics</subject><subject>Calcium - physiology</subject><subject>Cell Line, Transformed</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fibroblasts</subject><subject>Inositol Phosphates - biosynthesis</subject><subject>inositol trisphosphate</subject><subject>Isoenzymes - metabolism</subject><subject>Mutation</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - physiology</subject><subject>Phosphatidylinositol Phosphates - genetics</subject><subject>Phosphatidylinositol Phosphates - physiology</subject><subject>Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases</subject><subject>phospholipase C</subject><subject>Phospholipase C gamma</subject><subject>Phosphoproteins</subject><subject>Phosphoric Monoester Hydrolases - physiology</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - genetics</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases - physiology</subject><subject>Rats</subject><subject>receptor</subject><subject>Receptors, Antigen, B-Cell - metabolism</subject><subject>Receptors, IgG - physiology</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction - physiology</subject><subject>Type C Phospholipases - metabolism</subject><subject>Tyrosine - metabolism</subject><subject>tyrosine kinases</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1vEzEQXSFQCYUzJ6Q9IZC6icder9c9IEFU2kApkSiqlIvl9c5m3e5HsDeU_BN-Lg6JIjhVPoyl9zFv9KLoJZAxEMkm2Bb97QTEWIxBZvAoGkGakYQSwR9HI0IzSFLI5dPomfe3hBCeCziKjiSnKYAcRb_nde9XtR5suWls13s79E3CTtITngzOBmgHY_xmPpSzzu-xOXs7uUYT39lOe0xKXGFXYjfERjfGrtvY22Wng-MyXumhvteb01jHg3ZLHOKqd_G3i9k8abG0wbuMbVfbIqx2m73QP4-eVGHgi_08jr5_PLueXiSXX89n0_eXieGCykQXhUBu8jIvATXTOTWS50C5NlDQMkdAqAgYpsMPpcaKUSiB5SkVIqfAjqN3O9_VughxTLjB6UatnG2126heW_U_0tlaLfufCkAQntJg8Hpv4Pofa_SDaq032DS6w37tlZBCpJxlDxIhY5wLto002RGN6713WB3SAFHb1tXf1hUIJdS29aB49e8RB_6-5oDnO_zeNrh5yE6dffnwSXBJwgvSZCe1fsBfB6l2dyoTTHB1c3Wupgt6dbNYMPWZ_QGu6czE</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Scharenberg, Andrew M.</creator><creator>El-Hillal, Ousama</creator><creator>Fruman, David A.</creator><creator>Beitz, Laurie O.</creator><creator>Li, Zuomei</creator><creator>Lin, Siqi</creator><creator>Gout, Ivan</creator><creator>Cantley, Lewis C.</creator><creator>Rawlings, David J.</creator><creator>Kinet, Jean-Pierre</creator><general>John Wiley & Sons, Ltd</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>7QP</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980401</creationdate><title>Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals</title><author>Scharenberg, Andrew M. ; El-Hillal, Ousama ; Fruman, David A. ; Beitz, Laurie O. ; Li, Zuomei ; Lin, Siqi ; Gout, Ivan ; Cantley, Lewis C. ; Rawlings, David J. ; Kinet, Jean-Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5729-abb7e5c8d8d1ea3a82c958125ac1b2d8e1e1f01c3ae1ee9aef321d13842778213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>B-cells</topic><topic>Blood Proteins - genetics</topic><topic>Calcium - physiology</topic><topic>Cell Line, Transformed</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fibroblasts</topic><topic>Inositol Phosphates - biosynthesis</topic><topic>inositol trisphosphate</topic><topic>Isoenzymes - metabolism</topic><topic>Mutation</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - physiology</topic><topic>Phosphatidylinositol Phosphates - genetics</topic><topic>Phosphatidylinositol Phosphates - physiology</topic><topic>Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases</topic><topic>phospholipase C</topic><topic>Phospholipase C gamma</topic><topic>Phosphoproteins</topic><topic>Phosphoric Monoester Hydrolases - physiology</topic><topic>Phosphorylation</topic><topic>Protein-Tyrosine Kinases - genetics</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Protein-Tyrosine Kinases - physiology</topic><topic>Rats</topic><topic>receptor</topic><topic>Receptors, Antigen, B-Cell - metabolism</topic><topic>Receptors, IgG - physiology</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction - physiology</topic><topic>Type C Phospholipases - metabolism</topic><topic>Tyrosine - metabolism</topic><topic>tyrosine kinases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scharenberg, Andrew M.</creatorcontrib><creatorcontrib>El-Hillal, Ousama</creatorcontrib><creatorcontrib>Fruman, David A.</creatorcontrib><creatorcontrib>Beitz, Laurie O.</creatorcontrib><creatorcontrib>Li, Zuomei</creatorcontrib><creatorcontrib>Lin, Siqi</creatorcontrib><creatorcontrib>Gout, Ivan</creatorcontrib><creatorcontrib>Cantley, Lewis C.</creatorcontrib><creatorcontrib>Rawlings, David J.</creatorcontrib><creatorcontrib>Kinet, Jean-Pierre</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - 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>Scharenberg, Andrew M.</au><au>El-Hillal, Ousama</au><au>Fruman, David A.</au><au>Beitz, Laurie O.</au><au>Li, Zuomei</au><au>Lin, Siqi</au><au>Gout, Ivan</au><au>Cantley, Lewis C.</au><au>Rawlings, David J.</au><au>Kinet, Jean-Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1998-04-01</date><risdate>1998</risdate><volume>17</volume><issue>7</issue><spage>1961</spage><epage>1972</epage><pages>1961-1972</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><abstract>Tec family non‐receptor tyrosine kinases have been implicated in signal transduction events initiated by cell surface receptors from a broad range of cell types, including an essential role in B‐cell development. A unique feature of several Tec members among known tyrosine kinases is the presence of an N‐terminal pleckstrin homology (PH) domain. We directly demonstrate that phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns‐3,4,5‐P3) interacting with the PH domain acts as an upstream activation signal for Tec kinases, resulting in Tec kinase‐dependent phospholipase Cγ (PLCγ) tyrosine phosphorylation and inositol trisphosphate production. In addition, we show that this pathway is blocked when an SH2‐containing inositol phosphatase (SHIP)‐dependent inhibitory receptor is engaged. Together, our results suggest a general mechanism whereby PtdIns‐3,4,5‐P3 regulates receptor‐dependent calcium signals through the function of Tec kinases.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>9524119</pmid><doi>10.1093/emboj/17.7.1961</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals B-cells Blood Proteins - genetics Calcium - physiology Cell Line, Transformed Enzyme Activation Enzyme Inhibitors - pharmacology Fibroblasts Inositol Phosphates - biosynthesis inositol trisphosphate Isoenzymes - metabolism Mutation Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - physiology Phosphatidylinositol Phosphates - genetics Phosphatidylinositol Phosphates - physiology Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases phospholipase C Phospholipase C gamma Phosphoproteins Phosphoric Monoester Hydrolases - physiology Phosphorylation Protein-Tyrosine Kinases - genetics Protein-Tyrosine Kinases - metabolism Protein-Tyrosine Kinases - physiology Rats receptor Receptors, Antigen, B-Cell - metabolism Receptors, IgG - physiology Sequence Homology, Amino Acid Signal Transduction - physiology Type C Phospholipases - metabolism Tyrosine - metabolism tyrosine kinases |
| title | Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals |
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