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Isolation and characterization of Drosophila homologue of MKP-3 which has a high substrate specificity toward ERK

DC FieldValueLanguage
dc.contributor.author안용호-
dc.date.accessioned2016-05-16T11:13:11Z-
dc.date.available2016-05-16T11:13:11Z-
dc.date.issued2002-
dc.identifier.issn0264-6021-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/144059-
dc.description.abstractA partial C-terminal cDNA sequence of a novel Drosophila mitogen-activated protein kinase phosphatase (MKP), designated DMKP-3, was identified from an epitope expressed sequence tag database, and the missing N-terminal cDNA fragment was cloned from a Drosophila cDNA library. DMKP-3 is a protein of 411 amino acids, with a calculated molecular mass of 45.8 kDa; the deduced amino acid sequence is most similar to that of mammalian MKP-3. Recombinant DMKP-3 produced in Escherichia coli retained intrinsic tyrosine phosphatase activity. In addition, DMKP-3 specifically inhibited extracellular-signal-regulated kinase (ERK) activity, but was without a significant affect on c-Jun N-terminal kinase (JNK) and p38 activities, when it was overexpressed in Schneider cells. DMKP-3 interacted specifically with Drosophila ERK (DERK) via its N-terminal domain. In addition, DMKP-3 specifically inhibited Elk-1-dependent trans-reporter gene expression in mammalian CV1 cells, and dephosphorylated activated mammalian ERK in vitro. DMKP-3 is uniquely localized in the cytoplasm within Schneider cells, and gene expression is tightly regulated during development. Thus DMKP-3 is a Drosophila homologue of mammalian MKP-3, and may play important roles in the regulation of various developmental processes.-
dc.description.statementOfResponsibilityopen-
dc.format.extent143~151-
dc.relation.isPartOfBIOCHEMICAL JOURNAL-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleIsolation and characterization of Drosophila homologue of MKP-3 which has a high substrate specificity toward ERK-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Biochemistry & Molecular Biology (생화학,분자생물학)-
dc.contributor.googleauthorSun Hong Kim-
dc.contributor.googleauthorHyung Bae Kwon-
dc.contributor.googleauthorYong Sik Kim-
dc.contributor.googleauthorJi Hwan Ryu-
dc.contributor.googleauthorKyung Sub Kim-
dc.contributor.googleauthorYongho Ahn-
dc.contributor.googleauthorWon Jae Lee-
dc.contributor.googleauthorand Kang Yell Choi-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA02249-
dc.relation.journalcodeJ00282-
dc.identifier.eissn1470-8728-
dc.subject.keyworddual-specificity phosphatase-
dc.subject.keywordJNK-
dc.subject.keywordMAP kinase-
dc.subject.keywordp38-
dc.subject.keywordRolled-
dc.contributor.alternativeNameAhn, Yong Ho-
dc.contributor.affiliatedAuthorAhn, Yong Ho-
dc.rights.accessRightsfree-
dc.citation.volume361-
dc.citation.number1-
dc.citation.startPage143-
dc.citation.endPage151-
dc.identifier.bibliographicCitationBIOCHEMICAL JOURNAL, Vol.361(1) : 143-151, 2002-
dc.identifier.rimsid55554-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers

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