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Article: Protein Kinase C α-mediated Negative Feedback Regulation Is Responsible for the Termination of Insulin-like Growth Factor I-induced Activation of Nuclear Phospholipase C β1 in Swiss 3T3 Cells

TitleProtein Kinase C α-mediated Negative Feedback Regulation Is Responsible for the Termination of Insulin-like Growth Factor I-induced Activation of Nuclear Phospholipase C β1 in Swiss 3T3 Cells
Authors
Issue Date2001
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2001, v. 276 n. 18, p. 14980-14986 How to Cite?
AbstractPrevious studies from several independent laboratories have demonstrated the existence of an autonomous phosphoinositide (PI) cycle within the nucleus, where it is involved in both cell proliferation and differentiation. Stimulation of Swiss 3T3 cells with insulin-like growth factor-I (IGF-I) has been shown to induce a transient and rapid increase in the activity of nuclear-localized phospholipase C (PLC) β1, which in turn leads to the production of inositol trisphosphate and diacylglycerol in the nucleus. Nuclear diacylglycerol provides the driving force for the nuclear translocation of protein kinase C (PKC) α. Here, we report that treatment of Swiss 3T3 cells with Go6976, a selective inhibitor of PKC α, caused a sustained elevation of IGF-I-stimulated nuclear PLC activity. A time course study revealed an inverse relationship between nuclear PKC activity and the activity of nuclear PLC in IGF-1-treated cells. A time-dependent association between PKC α and PLC β1 in the nucleus was also observed following IGF-I treatment. Two-dimensional phosphopeptide mapping and site-directed mutagenesis demonstrated that PKC promoted phosphorylation of PLC β1 at serine 887 in the nucleus of IGF-I-treated cells. Overexpression of either a PLC β1 mutant in which the PKC phosphorylation site Ser887 was replaced by alanine, or a dominant-negative PKC α, resulted in a sustained activation of nuclear PLC following IGF-I stimulation. These results indicate that a negative feedback regulation of PLC β1 by PKC α plays a critical role in the termination of the IGF-I-dependent signal that activates the nuclear PI cycle.
Persistent Identifierhttp://hdl.handle.net/10722/162551
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXu, Aen_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorXu, LYen_HK
dc.contributor.authorGilmour, RSen_HK
dc.date.accessioned2012-09-05T05:20:59Z-
dc.date.available2012-09-05T05:20:59Z-
dc.date.issued2001en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2001, v. 276 n. 18, p. 14980-14986en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162551-
dc.description.abstractPrevious studies from several independent laboratories have demonstrated the existence of an autonomous phosphoinositide (PI) cycle within the nucleus, where it is involved in both cell proliferation and differentiation. Stimulation of Swiss 3T3 cells with insulin-like growth factor-I (IGF-I) has been shown to induce a transient and rapid increase in the activity of nuclear-localized phospholipase C (PLC) β1, which in turn leads to the production of inositol trisphosphate and diacylglycerol in the nucleus. Nuclear diacylglycerol provides the driving force for the nuclear translocation of protein kinase C (PKC) α. Here, we report that treatment of Swiss 3T3 cells with Go6976, a selective inhibitor of PKC α, caused a sustained elevation of IGF-I-stimulated nuclear PLC activity. A time course study revealed an inverse relationship between nuclear PKC activity and the activity of nuclear PLC in IGF-1-treated cells. A time-dependent association between PKC α and PLC β1 in the nucleus was also observed following IGF-I treatment. Two-dimensional phosphopeptide mapping and site-directed mutagenesis demonstrated that PKC promoted phosphorylation of PLC β1 at serine 887 in the nucleus of IGF-I-treated cells. Overexpression of either a PLC β1 mutant in which the PKC phosphorylation site Ser887 was replaced by alanine, or a dominant-negative PKC α, resulted in a sustained activation of nuclear PLC following IGF-I stimulation. These results indicate that a negative feedback regulation of PLC β1 by PKC α plays a critical role in the termination of the IGF-I-dependent signal that activates the nuclear PI cycle.en_HK
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subject.mesh3T3 Cellsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCell Nucleus - Enzymologyen_US
dc.subject.meshDna Primersen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshEnzyme Inhibitors - Pharmacologyen_US
dc.subject.meshFeedbacken_US
dc.subject.meshInsulin-Like Growth Factor I - Pharmacologyen_US
dc.subject.meshIsoenzymes - Antagonists & Inhibitors - Genetics - Metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshPhospholipase C Betaen_US
dc.subject.meshProtein Kinase C - Antagonists & Inhibitors - Metabolismen_US
dc.subject.meshProtein Kinase C-Alphaen_US
dc.subject.meshSerine - Metabolismen_US
dc.subject.meshType C Phospholipases - Genetics - Metabolismen_US
dc.titleProtein Kinase C α-mediated Negative Feedback Regulation Is Responsible for the Termination of Insulin-like Growth Factor I-induced Activation of Nuclear Phospholipase C β1 in Swiss 3T3 Cellsen_HK
dc.typeArticleen_HK
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M009144200en_HK
dc.identifier.pmid11278470-
dc.identifier.scopuseid_2-s2.0-0035805635en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035805635&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume276en_HK
dc.identifier.issue18en_HK
dc.identifier.spage14980en_HK
dc.identifier.epage14986en_HK
dc.identifier.isiWOS:000168528800062-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, LY=7404744252en_HK
dc.identifier.scopusauthoridGilmour, RS=7102979590en_HK

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