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Isolation and characterization of Drosophila homologue of MKP-3 which has a high substrate specificity toward ERK
DC Field | Value | Language |
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dc.contributor.author | 안용호 | - |
dc.date.accessioned | 2016-05-16T11:13:11Z | - |
dc.date.available | 2016-05-16T11:13:11Z | - |
dc.date.issued | 2002 | - |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/144059 | - |
dc.description.abstract | A 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.statementOfResponsibility | open | - |
dc.format.extent | 143~151 | - |
dc.relation.isPartOf | BIOCHEMICAL JOURNAL | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | Isolation and characterization of Drosophila homologue of MKP-3 which has a high substrate specificity toward ERK | - |
dc.type | Article | - |
dc.contributor.college | College of Medicine (의과대학) | - |
dc.contributor.department | Dept. of Biochemistry & Molecular Biology (생화학,분자생물학) | - |
dc.contributor.googleauthor | Sun Hong Kim | - |
dc.contributor.googleauthor | Hyung Bae Kwon | - |
dc.contributor.googleauthor | Yong Sik Kim | - |
dc.contributor.googleauthor | Ji Hwan Ryu | - |
dc.contributor.googleauthor | Kyung Sub Kim | - |
dc.contributor.googleauthor | Yongho Ahn | - |
dc.contributor.googleauthor | Won Jae Lee | - |
dc.contributor.googleauthor | and Kang Yell Choi | - |
dc.admin.author | false | - |
dc.admin.mapping | false | - |
dc.contributor.localId | A02249 | - |
dc.relation.journalcode | J00282 | - |
dc.identifier.eissn | 1470-8728 | - |
dc.subject.keyword | dual-specificity phosphatase | - |
dc.subject.keyword | JNK | - |
dc.subject.keyword | MAP kinase | - |
dc.subject.keyword | p38 | - |
dc.subject.keyword | Rolled | - |
dc.contributor.alternativeName | Ahn, Yong Ho | - |
dc.contributor.affiliatedAuthor | Ahn, Yong Ho | - |
dc.rights.accessRights | free | - |
dc.citation.volume | 361 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 143 | - |
dc.citation.endPage | 151 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL JOURNAL, Vol.361(1) : 143-151, 2002 | - |
dc.identifier.rimsid | 55554 | - |
dc.type.rims | ART | - |
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