Signaling by Distinct Classes of Phosphoinositide 3-Kinases
Many signaling pathways converge on and regulate phosphoinositide 3-kinase (PI3K) enzymes whose inositol lipid products are key mediators of intracellular signaling. Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affe...
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Veröffentlicht in: | Experimental cell research 1999-11, Vol.253 (1), p.239-254 |
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description | Many signaling pathways converge on and regulate phosphoinositide 3-kinase (PI3K) enzymes whose inositol lipid products are key mediators of intracellular signaling. Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affecting their localization, conformation, and activities. Here we review the activation mechanisms of the different types of PI3Ks and their downstream actions, with focus on the PI3Ks that are acutely triggered by extracellular stimulation. |
doi_str_mv | 10.1006/excr.1999.4701 |
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Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affecting their localization, conformation, and activities. 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Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affecting their localization, conformation, and activities. Here we review the activation mechanisms of the different types of PI3Ks and their downstream actions, with focus on the PI3Ks that are acutely triggered by extracellular stimulation.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Isoenzymes - antagonists & inhibitors</subject><subject>Isoenzymes - classification</subject><subject>Isoenzymes - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</subject><subject>Phosphatidylinositol 3-Kinases - classification</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Signal Transduction</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EoqWwMqJMbAlnx3FiMaHyKSqBBMxW4pxbozQudorovydROrAw3XDP--ruIeScQkIBxBX-aJ9QKWXCc6AHZEpBQsw4Y4dkCkB5zAuWT8hJCJ8AUBRUHJMJhSyXkokpuX6zy7ZsbLuMql10a0NnW91F86YMAUPkTPS6cmGzcrZ1wXa2xiiNn21b9ttTcmTKJuDZfs7Ix_3d-_wxXrw8PM1vFrHmILo4E1XWH8VSQammlUwpTwUKYbBCXmUVN4LlkqZZxiVnueEmN1CiFIXASguTzsjl2Lvx7muLoVNrGzQ2Tdmi2wYlZMpAFNCDyQhq70LwaNTG23Xpd4qCGnSpQZcadKlBVx-42DdvqzXWf_DRTw8UI4D9f98WvQraYquxth51p2pn_-v-BeBOeBY</recordid><startdate>19991125</startdate><enddate>19991125</enddate><creator>Vanhaesebroeck, B.</creator><creator>Waterfield, M.D.</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>19991125</creationdate><title>Signaling by Distinct Classes of Phosphoinositide 3-Kinases</title><author>Vanhaesebroeck, B. ; Waterfield, M.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-56b509023611c1b931436e66febe4b5b4f6279135549427f4f7f0ae9686ebc6f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Isoenzymes - antagonists & inhibitors</topic><topic>Isoenzymes - classification</topic><topic>Isoenzymes - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Phosphatidylinositol 3-Kinases - antagonists & inhibitors</topic><topic>Phosphatidylinositol 3-Kinases - classification</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Signal Transduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vanhaesebroeck, B.</creatorcontrib><creatorcontrib>Waterfield, M.D.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vanhaesebroeck, B.</au><au>Waterfield, M.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Signaling by Distinct Classes of Phosphoinositide 3-Kinases</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1999-11-25</date><risdate>1999</risdate><volume>253</volume><issue>1</issue><spage>239</spage><epage>254</epage><pages>239-254</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><abstract>Many signaling pathways converge on and regulate phosphoinositide 3-kinase (PI3K) enzymes whose inositol lipid products are key mediators of intracellular signaling. Different PI3K isoforms generate specific lipids that bind to FYVE and pleckstrin homology (PH) domains in a variety of proteins, affecting their localization, conformation, and activities. Here we review the activation mechanisms of the different types of PI3Ks and their downstream actions, with focus on the PI3Ks that are acutely triggered by extracellular stimulation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10579926</pmid><doi>10.1006/excr.1999.4701</doi><tpages>16</tpages></addata></record> |
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subjects | Animals Binding Sites Isoenzymes - antagonists & inhibitors Isoenzymes - classification Isoenzymes - metabolism Mice Mice, Knockout Phosphatidylinositol 3-Kinases - antagonists & inhibitors Phosphatidylinositol 3-Kinases - classification Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism Protein Structure, Tertiary Protein-Serine-Threonine Kinases - metabolism Signal Transduction |
title | Signaling by Distinct Classes of Phosphoinositide 3-Kinases |
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