PLC regulation: emerging pictures for molecular mechanisms

Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G pro...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Trends in biochemical sciences (Amsterdam. Regular ed.) 2011-02, Vol.36 (2), p.88-96
Hauptverfasser: Bunney, Tom D., Katan, Matilda
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 96
container_issue 2
container_start_page 88
container_title Trends in biochemical sciences (Amsterdam. Regular ed.)
container_volume 36
creator Bunney, Tom D.
Katan, Matilda
description Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.
doi_str_mv 10.1016/j.tibs.2010.08.003
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_851478640</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0968000410001660</els_id><sourcerecordid>851478640</sourcerecordid><originalsourceid>FETCH-LOGICAL-c379t-677914cc6a07662c519588a4c115ac306ed9786f01ca7fc56fc7588be0a8e3</originalsourceid><addsrcrecordid>eNp9kE1LAzEQhoMotlb_gAfdm6etk_1IssWLFL-goPhxDul0tqbsR012Bf-9KasePc0wPO_L8DB2ymHKgYvLzbSzSz9NIBxATQHSPTbmqUjiLE3EPhtDIVQMANmIHXm_AeC5lPkhGyWgJGQcxmz2tJhHjtZ9ZTrbNrOIanJr26yjrcWud-SjsnVR3VaEgQkb4btprK_9MTsoTeXp5GdO2PPtzev8Pl483j3MrxcxprLoYiFlwTNEYUAKkWDOi1wpkyHnucEUBK0KqUQJHI0sMRclygAsCYyidMIuhtKtaz968p2urUeqKtNQ23utcp6FdAaBTAYSXeu9o1Jvna2N-9Ic9M6X3uidL73zpUHp4CuEzn7q-2VNq7_Ir6AAnA9AaVpt1s56_fYSGkTQCjwBEYirgaDg4NOS0x4tNUgr6wg7vWrtfx98AwTQhEI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>851478640</pqid></control><display><type>article</type><title>PLC regulation: emerging pictures for molecular mechanisms</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Collection</source><creator>Bunney, Tom D. ; Katan, Matilda</creator><creatorcontrib>Bunney, Tom D. ; Katan, Matilda</creatorcontrib><description>Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.</description><identifier>ISSN: 0968-0004</identifier><identifier>EISSN: 1362-4326</identifier><identifier>DOI: 10.1016/j.tibs.2010.08.003</identifier><identifier>PMID: 20870410</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Animals ; Cell Membrane - enzymology ; cell membranes ; Enzyme Activation ; GTP Phosphohydrolases - metabolism ; GTP-Binding Proteins - metabolism ; guanosinetriphosphatase ; Humans ; Models, Molecular ; Phosphoinositide Phospholipase C - chemistry ; Phosphoinositide Phospholipase C - metabolism ; phospholipase C ; phosphotransferases (kinases) ; protein subunits ; proteins ; receptors ; regulatory proteins ; Signal Transduction ; tyrosine</subject><ispartof>Trends in biochemical sciences (Amsterdam. Regular ed.), 2011-02, Vol.36 (2), p.88-96</ispartof><rights>2010 Elsevier Ltd</rights><rights>Copyright © 2010 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-677914cc6a07662c519588a4c115ac306ed9786f01ca7fc56fc7588be0a8e3</citedby><cites>FETCH-LOGICAL-c379t-677914cc6a07662c519588a4c115ac306ed9786f01ca7fc56fc7588be0a8e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0968000410001660$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20870410$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bunney, Tom D.</creatorcontrib><creatorcontrib>Katan, Matilda</creatorcontrib><title>PLC regulation: emerging pictures for molecular mechanisms</title><title>Trends in biochemical sciences (Amsterdam. Regular ed.)</title><addtitle>Trends Biochem Sci</addtitle><description>Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.</description><subject>Animals</subject><subject>Cell Membrane - enzymology</subject><subject>cell membranes</subject><subject>Enzyme Activation</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>guanosinetriphosphatase</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Phosphoinositide Phospholipase C - chemistry</subject><subject>Phosphoinositide Phospholipase C - metabolism</subject><subject>phospholipase C</subject><subject>phosphotransferases (kinases)</subject><subject>protein subunits</subject><subject>proteins</subject><subject>receptors</subject><subject>regulatory proteins</subject><subject>Signal Transduction</subject><subject>tyrosine</subject><issn>0968-0004</issn><issn>1362-4326</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LAzEQhoMotlb_gAfdm6etk_1IssWLFL-goPhxDul0tqbsR012Bf-9KasePc0wPO_L8DB2ymHKgYvLzbSzSz9NIBxATQHSPTbmqUjiLE3EPhtDIVQMANmIHXm_AeC5lPkhGyWgJGQcxmz2tJhHjtZ9ZTrbNrOIanJr26yjrcWud-SjsnVR3VaEgQkb4btprK_9MTsoTeXp5GdO2PPtzev8Pl483j3MrxcxprLoYiFlwTNEYUAKkWDOi1wpkyHnucEUBK0KqUQJHI0sMRclygAsCYyidMIuhtKtaz968p2urUeqKtNQ23utcp6FdAaBTAYSXeu9o1Jvna2N-9Ic9M6X3uidL73zpUHp4CuEzn7q-2VNq7_Ir6AAnA9AaVpt1s56_fYSGkTQCjwBEYirgaDg4NOS0x4tNUgr6wg7vWrtfx98AwTQhEI</recordid><startdate>20110201</startdate><enddate>20110201</enddate><creator>Bunney, Tom D.</creator><creator>Katan, Matilda</creator><general>Elsevier Ltd</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>20110201</creationdate><title>PLC regulation: emerging pictures for molecular mechanisms</title><author>Bunney, Tom D. ; Katan, Matilda</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-677914cc6a07662c519588a4c115ac306ed9786f01ca7fc56fc7588be0a8e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Cell Membrane - enzymology</topic><topic>cell membranes</topic><topic>Enzyme Activation</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>guanosinetriphosphatase</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Phosphoinositide Phospholipase C - chemistry</topic><topic>Phosphoinositide Phospholipase C - metabolism</topic><topic>phospholipase C</topic><topic>phosphotransferases (kinases)</topic><topic>protein subunits</topic><topic>proteins</topic><topic>receptors</topic><topic>regulatory proteins</topic><topic>Signal Transduction</topic><topic>tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bunney, Tom D.</creatorcontrib><creatorcontrib>Katan, Matilda</creatorcontrib><collection>AGRIS</collection><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>Trends in biochemical sciences (Amsterdam. Regular ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bunney, Tom D.</au><au>Katan, Matilda</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PLC regulation: emerging pictures for molecular mechanisms</atitle><jtitle>Trends in biochemical sciences (Amsterdam. Regular ed.)</jtitle><addtitle>Trends Biochem Sci</addtitle><date>2011-02-01</date><risdate>2011</risdate><volume>36</volume><issue>2</issue><spage>88</spage><epage>96</epage><pages>88-96</pages><issn>0968-0004</issn><eissn>1362-4326</eissn><abstract>Phosphoinositide-specific phospholipase C (PLC) enzymes are common signalling components linked to the activation of most cellular receptors. All PLC families are complex, modular, multi-domain proteins and together cover a broad spectrum of regulatory interactions, including direct binding to G protein subunits, small GTPases from Rho and Ras families, receptor and non-receptor tyrosine kinases and lipid components of cellular membranes. Recent structural determinations of PLC components and their complexes with regulatory proteins and direct mechanistic studies, together with earlier work, have provided the foundation to propose molecular mechanisms that stringently regulate PLC activity.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>20870410</pmid><doi>10.1016/j.tibs.2010.08.003</doi><tpages>9</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0968-0004
ispartof Trends in biochemical sciences (Amsterdam. Regular ed.), 2011-02, Vol.36 (2), p.88-96
issn 0968-0004
1362-4326
language eng
recordid cdi_proquest_miscellaneous_851478640
source MEDLINE; Elsevier ScienceDirect Journals Collection
subjects Animals
Cell Membrane - enzymology
cell membranes
Enzyme Activation
GTP Phosphohydrolases - metabolism
GTP-Binding Proteins - metabolism
guanosinetriphosphatase
Humans
Models, Molecular
Phosphoinositide Phospholipase C - chemistry
Phosphoinositide Phospholipase C - metabolism
phospholipase C
phosphotransferases (kinases)
protein subunits
proteins
receptors
regulatory proteins
Signal Transduction
tyrosine
title PLC regulation: emerging pictures for molecular mechanisms
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T15%3A05%3A44IST&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=PLC%20regulation:%20emerging%20pictures%20for%20molecular%20mechanisms&rft.jtitle=Trends%20in%20biochemical%20sciences%20(Amsterdam.%20Regular%20ed.)&rft.au=Bunney,%20Tom%20D.&rft.date=2011-02-01&rft.volume=36&rft.issue=2&rft.spage=88&rft.epage=96&rft.pages=88-96&rft.issn=0968-0004&rft.eissn=1362-4326&rft_id=info:doi/10.1016/j.tibs.2010.08.003&rft_dat=%3Cproquest_cross%3E851478640%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=851478640&rft_id=info:pmid/20870410&rft_els_id=S0968000410001660&rfr_iscdi=true