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Article: Identification of a novel Inhibitor of Differentiation-1 (ID-1) binding partner, caveolin-1, and its role in epithelial-mesenchymal transition and resistance to apoptosis in prostate cancer cells

TitleIdentification of a novel Inhibitor of Differentiation-1 (ID-1) binding partner, caveolin-1, and its role in epithelial-mesenchymal transition and resistance to apoptosis in prostate cancer cells
Authors
Issue Date2007
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, 2007, v. 282 n. 46, p. 33284-33294 How to Cite?
AbstractRecently, ID-1 (inhibitor of differentiation/DNA binding) is suggested as an oncogene and is reported to promote cell proliferation, invasion, and survival in several types of human cancer cells through multiple signaling pathways. However, how Id-1 interacts with these pathways and the immediate downstream effectors of the Id-1 protein are not known. In this study, using a yeast two-hybrid screening technique, we identified a novel Id-1-interacting protein, caveolin-1 (Cav-1), a cell membrane protein, and a positive regulator of cell survival and metastasis in prostate cancer. Using an immunoprecipitation method, we found that the helix-loop-helix domain of the Id-1 protein was essential for the physical interaction between Id-1 and Cav-1. In addition, we also demonstrated that the physical interaction between Id-1 and Cav-1 played a key role in the epithelial-mesenchymal transition and increased cell migration rate as well as resistance to taxol-induced apoptosis in prostate cancer cells. Furthermore, our results revealed that this effect was regulated by Id-1-induced Akt activation through promoting the binding activity between Cav-1 and protein phosphatase 2A. Our study demonstrates a novel Id-1 binding partner and suggests a molecular mechanism that mediates the function of Id-1 in promoting prostate cancer progression through activation of the Akt pathway leading to cancer cell invasion and resistance to anticancer drug-induced apoptosis. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/67985
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Xen_HK
dc.contributor.authorLing, MTen_HK
dc.contributor.authorWang, Qen_HK
dc.contributor.authorLau, CKen_HK
dc.contributor.authorLeung, SCLen_HK
dc.contributor.authorLee, TKen_HK
dc.contributor.authorCheung, ALMen_HK
dc.contributor.authorWong, YCen_HK
dc.contributor.authorWang, Xen_HK
dc.date.accessioned2010-09-06T06:00:05Z-
dc.date.available2010-09-06T06:00:05Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2007, v. 282 n. 46, p. 33284-33294en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/67985-
dc.description.abstractRecently, ID-1 (inhibitor of differentiation/DNA binding) is suggested as an oncogene and is reported to promote cell proliferation, invasion, and survival in several types of human cancer cells through multiple signaling pathways. However, how Id-1 interacts with these pathways and the immediate downstream effectors of the Id-1 protein are not known. In this study, using a yeast two-hybrid screening technique, we identified a novel Id-1-interacting protein, caveolin-1 (Cav-1), a cell membrane protein, and a positive regulator of cell survival and metastasis in prostate cancer. Using an immunoprecipitation method, we found that the helix-loop-helix domain of the Id-1 protein was essential for the physical interaction between Id-1 and Cav-1. In addition, we also demonstrated that the physical interaction between Id-1 and Cav-1 played a key role in the epithelial-mesenchymal transition and increased cell migration rate as well as resistance to taxol-induced apoptosis in prostate cancer cells. Furthermore, our results revealed that this effect was regulated by Id-1-induced Akt activation through promoting the binding activity between Cav-1 and protein phosphatase 2A. Our study demonstrates a novel Id-1 binding partner and suggests a molecular mechanism that mediates the function of Id-1 in promoting prostate cancer progression through activation of the Akt pathway leading to cancer cell invasion and resistance to anticancer drug-induced apoptosis. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
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.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshApoptosisen_HK
dc.subject.meshCaveolin 1 - metabolismen_HK
dc.subject.meshCell Movementen_HK
dc.subject.meshDrug Resistance, Neoplasmen_HK
dc.subject.meshEpithelium - metabolismen_HK
dc.subject.meshGene Expression Regulation, Neoplasticen_HK
dc.subject.meshHumansen_HK
dc.subject.meshInhibitor of Differentiation Protein 1 - metabolismen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMesoderm - metabolismen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNeoplasm Invasivenessen_HK
dc.subject.meshPaclitaxel - pharmacologyen_HK
dc.subject.meshProstatic Neoplasms - metabolism - pathologyen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshTwo-Hybrid System Techniquesen_HK
dc.titleIdentification of a novel Inhibitor of Differentiation-1 (ID-1) binding partner, caveolin-1, and its role in epithelial-mesenchymal transition and resistance to apoptosis in prostate cancer cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=282&issue=46&spage=33284&epage=33294&date=2007&atitle=Identification+of+a+novel+inhibitor+of+differentiation-1+(ID-1)+binding+partner,+caveolin-1,+and+its+role+in+epithelial-mesenchymal+transition+and+resistance+to+apoptosis+in+prostate+cancer+cellsen_HK
dc.identifier.emailLing, MT:patling@hkucc.hku.hken_HK
dc.identifier.emailLee, TK:tkwlee@hkucc.hku.hken_HK
dc.identifier.emailCheung, ALM:lmcheung@hkucc.hku.hken_HK
dc.identifier.emailWong, YC:ycwong@hkucc.hku.hken_HK
dc.identifier.authorityLing, MT=rp00449en_HK
dc.identifier.authorityLee, TK=rp00447en_HK
dc.identifier.authorityCheung, ALM=rp00332en_HK
dc.identifier.authorityWong, YC=rp00316en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/jbc.M705089200en_HK
dc.identifier.pmid17855368-
dc.identifier.scopuseid_2-s2.0-36348964327en_HK
dc.identifier.hkuros138888en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-36348964327&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume282en_HK
dc.identifier.issue46en_HK
dc.identifier.spage33284en_HK
dc.identifier.epage33294en_HK
dc.identifier.isiWOS:000250840200008-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhang, X=8578540900en_HK
dc.identifier.scopusauthoridLing, MT=7102229780en_HK
dc.identifier.scopusauthoridWang, Q=7408172643en_HK
dc.identifier.scopusauthoridLau, CK=7401968442en_HK
dc.identifier.scopusauthoridLeung, SCL=36894169100en_HK
dc.identifier.scopusauthoridLee, TK=7501439435en_HK
dc.identifier.scopusauthoridCheung, ALM=7401806497en_HK
dc.identifier.scopusauthoridWong, YC=7403041798en_HK
dc.identifier.scopusauthoridWang, X=7501854829en_HK
dc.identifier.citeulike1850943-

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