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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Experimental cell research 1999-11, Vol.253 (1), p.239-254
Hauptverfasser: Vanhaesebroeck, B., Waterfield, M.D.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 254
container_issue 1
container_start_page 239
container_title Experimental cell research
container_volume 253
creator Vanhaesebroeck, B.
Waterfield, M.D.
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69320680</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014482799947018</els_id><sourcerecordid>69320680</sourcerecordid><originalsourceid>FETCH-LOGICAL-c406t-56b509023611c1b931436e66febe4b5b4f6279135549427f4f7f0ae9686ebc6f3</originalsourceid><addsrcrecordid>eNp1kD1PwzAQhi0EoqWwMqJMbAlnx3FiMaHyKSqBBMxW4pxbozQudorovydROrAw3XDP--ruIeScQkIBxBX-aJ9QKWXCc6AHZEpBQsw4Y4dkCkB5zAuWT8hJCJ8AUBRUHJMJhSyXkokpuX6zy7ZsbLuMql10a0NnW91F86YMAUPkTPS6cmGzcrZ1wXa2xiiNn21b9ttTcmTKJuDZfs7Ix_3d-_wxXrw8PM1vFrHmILo4E1XWH8VSQammlUwpTwUKYbBCXmUVN4LlkqZZxiVnueEmN1CiFIXASguTzsjl2Lvx7muLoVNrGzQ2Tdmi2wYlZMpAFNCDyQhq70LwaNTG23Xpd4qCGnSpQZcadKlBVx-42DdvqzXWf_DRTw8UI4D9f98WvQraYquxth51p2pn_-v-BeBOeBY</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69320680</pqid></control><display><type>article</type><title>Signaling by Distinct Classes of Phosphoinositide 3-Kinases</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Vanhaesebroeck, B. ; Waterfield, M.D.</creator><creatorcontrib>Vanhaesebroeck, B. ; Waterfield, M.D.</creatorcontrib><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.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1006/excr.1999.4701</identifier><identifier>PMID: 10579926</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Binding Sites ; Isoenzymes - antagonists &amp; inhibitors ; Isoenzymes - classification ; Isoenzymes - metabolism ; Mice ; Mice, Knockout ; Phosphatidylinositol 3-Kinases - antagonists &amp; inhibitors ; Phosphatidylinositol 3-Kinases - classification ; Phosphatidylinositol 3-Kinases - genetics ; Phosphatidylinositol 3-Kinases - metabolism ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases - metabolism ; Signal Transduction</subject><ispartof>Experimental cell research, 1999-11, Vol.253 (1), p.239-254</ispartof><rights>1999 Academic Press</rights><rights>Copyright 1999 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-56b509023611c1b931436e66febe4b5b4f6279135549427f4f7f0ae9686ebc6f3</citedby><cites>FETCH-LOGICAL-c406t-56b509023611c1b931436e66febe4b5b4f6279135549427f4f7f0ae9686ebc6f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014482799947018$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10579926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vanhaesebroeck, B.</creatorcontrib><creatorcontrib>Waterfield, M.D.</creatorcontrib><title>Signaling by Distinct Classes of Phosphoinositide 3-Kinases</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><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.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Isoenzymes - antagonists &amp; inhibitors</subject><subject>Isoenzymes - classification</subject><subject>Isoenzymes - metabolism</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Phosphatidylinositol 3-Kinases - antagonists &amp; 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 &amp; inhibitors</topic><topic>Isoenzymes - classification</topic><topic>Isoenzymes - metabolism</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Phosphatidylinositol 3-Kinases - antagonists &amp; 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>
fulltext fulltext
identifier ISSN: 0014-4827
ispartof Experimental cell research, 1999-11, Vol.253 (1), p.239-254
issn 0014-4827
1090-2422
language eng
recordid cdi_proquest_miscellaneous_69320680
source MEDLINE; Elsevier ScienceDirect Journals
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T17%3A32%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Signaling%20by%20Distinct%20Classes%20of%20Phosphoinositide%203-Kinases&rft.jtitle=Experimental%20cell%20research&rft.au=Vanhaesebroeck,%20B.&rft.date=1999-11-25&rft.volume=253&rft.issue=1&rft.spage=239&rft.epage=254&rft.pages=239-254&rft.issn=0014-4827&rft.eissn=1090-2422&rft_id=info:doi/10.1006/excr.1999.4701&rft_dat=%3Cproquest_cross%3E69320680%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69320680&rft_id=info:pmid/10579926&rft_els_id=S0014482799947018&rfr_iscdi=true