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Article: The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases

TitleThe zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases
Authors
Issue Date1999
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/onc
Citation
Oncogene, 1999, v. 18 n. 29, p. 4182-4190 How to Cite?
AbstractA20 is a Cys2/Cys2 zinc finger protein which is induced by a variety of inflammatory stimuli and which has been characterized as an inhibitor of cell death by a yet unknown mechanism. In order to clarify its molecular mechanism of action, we used the yeast two-hybrid system to screen for proteins that interact with A20. A cDNA fragment was isolated which encoded a portion of a novel protein (TXBP151), which was recently found to be a human T-cell leukemia virus type-I (HTLV-I) Tax-binding protein. The full-length 2386 bp TXBP151 mRNA encodes a protein of 86 kDa. Like A20, overexpression of TXBP151 could inhibit apoptosis induced by tumour necrosis factor (TNF) in NIH3T3 cells. Moreover, transfection of antisense TXBP151 partially abolished the anti-apoptotic effect of A20. Furthermore, apoptosis induced by TNF or CD95 (Fas/APO-1) was associated with proteolysis of TXBP151. This degradation could be inhibited by the broad-spectrum caspase inhibitor zVAD-fmk or by expression of the cowpox virus-derived inhibitor CrmA, suggesting that TXBP151 is a novel substrate for caspase family members. TXBP151 was indeed found to be specifically cleaved in vitro by members of the caspase-3-like subfamily, viz. caspase-3, caspase-6 and caspase-7. Thus TXBP151 appears to be a novel A20-binding protein which might mediate the anti-apoptotic activity of A20, and which can be processed by specific caspases.
Persistent Identifierhttp://hdl.handle.net/10722/108849
ISSN
2015 Impact Factor: 7.932
2015 SCImago Journal Rankings: 4.047
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDe Valck, Den_HK
dc.contributor.authorJin, DYen_HK
dc.contributor.authorHeyninck, Ken_HK
dc.contributor.authorVan De Craen, Men_HK
dc.contributor.authorContreras, Ren_HK
dc.contributor.authorFiers, Wen_HK
dc.contributor.authorJeang, KTen_HK
dc.contributor.authorBeyaert, Ren_HK
dc.date.accessioned2010-09-26T00:57:07Z-
dc.date.available2010-09-26T00:57:07Z-
dc.date.issued1999en_HK
dc.identifier.citationOncogene, 1999, v. 18 n. 29, p. 4182-4190en_HK
dc.identifier.issn0950-9232en_HK
dc.identifier.urihttp://hdl.handle.net/10722/108849-
dc.description.abstractA20 is a Cys2/Cys2 zinc finger protein which is induced by a variety of inflammatory stimuli and which has been characterized as an inhibitor of cell death by a yet unknown mechanism. In order to clarify its molecular mechanism of action, we used the yeast two-hybrid system to screen for proteins that interact with A20. A cDNA fragment was isolated which encoded a portion of a novel protein (TXBP151), which was recently found to be a human T-cell leukemia virus type-I (HTLV-I) Tax-binding protein. The full-length 2386 bp TXBP151 mRNA encodes a protein of 86 kDa. Like A20, overexpression of TXBP151 could inhibit apoptosis induced by tumour necrosis factor (TNF) in NIH3T3 cells. Moreover, transfection of antisense TXBP151 partially abolished the anti-apoptotic effect of A20. Furthermore, apoptosis induced by TNF or CD95 (Fas/APO-1) was associated with proteolysis of TXBP151. This degradation could be inhibited by the broad-spectrum caspase inhibitor zVAD-fmk or by expression of the cowpox virus-derived inhibitor CrmA, suggesting that TXBP151 is a novel substrate for caspase family members. TXBP151 was indeed found to be specifically cleaved in vitro by members of the caspase-3-like subfamily, viz. caspase-3, caspase-6 and caspase-7. Thus TXBP151 appears to be a novel A20-binding protein which might mediate the anti-apoptotic activity of A20, and which can be processed by specific caspases.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/oncen_HK
dc.relation.ispartofOncogeneen_HK
dc.subject.mesh3T3 Cellsen_HK
dc.subject.meshAmino Acid Chloromethyl Ketones - pharmacologyen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAntigens, CD95 - physiologyen_HK
dc.subject.meshApoptosis - drug effectsen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshCarrier Proteins - isolation & purification - metabolismen_HK
dc.subject.meshCaspases - metabolismen_HK
dc.subject.meshCell Lineen_HK
dc.subject.meshCloning, Molecularen_HK
dc.subject.meshCysteine Endopeptidasesen_HK
dc.subject.meshCysteine Proteinase Inhibitors - pharmacologyen_HK
dc.subject.meshDNA, Complementary - geneticsen_HK
dc.subject.meshDactinomycin - pharmacologyen_HK
dc.subject.meshGenesen_HK
dc.subject.meshHeLa Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshIntracellular Signaling Peptides and Proteinsen_HK
dc.subject.meshMiceen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNeoplasm Proteinsen_HK
dc.subject.meshNuclear Proteinsen_HK
dc.subject.meshNucleic Acid Synthesis Inhibitors - pharmacologyen_HK
dc.subject.meshOligonucleotides, Antisense - pharmacologyen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Processing, Post-Translationalen_HK
dc.subject.meshProteins - metabolismen_HK
dc.subject.meshRNA, Messenger - geneticsen_HK
dc.subject.meshRecombinant Fusion Proteins - metabolismen_HK
dc.subject.meshSaccharomyces cerevisiae - geneticsen_HK
dc.subject.meshSerpins - physiologyen_HK
dc.subject.meshSubstrate Specificityen_HK
dc.subject.meshTransfectionen_HK
dc.subject.meshTumor Necrosis Factor-alpha - pharmacologyen_HK
dc.subject.meshViral Proteinsen_HK
dc.subject.meshZinc Fingersen_HK
dc.titleThe zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspasesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0950-9232&volume=18&issue=29&spage=4182&epage=4190&date=1999&atitle=The+zinc+finger+protein+A20+interacts+with+a+novel+anti-apoptotic+protein+which+is+cleaved+by+specific+caspasesen_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/sj.onc.1202787en_HK
dc.identifier.pmid10435631-
dc.identifier.scopuseid_2-s2.0-0033595143en_HK
dc.identifier.hkuros46216en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033595143&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume18en_HK
dc.identifier.issue29en_HK
dc.identifier.spage4182en_HK
dc.identifier.epage4190en_HK
dc.identifier.isiWOS:000081542400002-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridDe Valck, D=6603395009en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK
dc.identifier.scopusauthoridHeyninck, K=6602089969en_HK
dc.identifier.scopusauthoridVan De Craen, M=6603637935en_HK
dc.identifier.scopusauthoridContreras, R=7202407035en_HK
dc.identifier.scopusauthoridFiers, W=35593837000en_HK
dc.identifier.scopusauthoridJeang, KT=7004824803en_HK
dc.identifier.scopusauthoridBeyaert, R=7005325142en_HK

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