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

Authors
 Sun Hong Kim  ;  Hyung Bae Kwon  ;  Yong Sik Kim  ;  Ji Hwan Ryu  ;  Kyung Sub Kim  ;  Yongho Ahn  ;  Won Jae Lee  ;  and Kang Yell Choi 
Citation
 BIOCHEMICAL JOURNAL, Vol.361(1) : 143-151, 2002 
Journal Title
 BIOCHEMICAL JOURNAL 
ISSN
 0264-6021 
Issue Date
2002
Keywords
dual-specificity phosphatase ; JNK ; MAP kinase ; p38 ; Rolled
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.
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Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
Yonsei Authors
Ahn, Yong Ho(안용호) ORCID logo https://orcid.org/0000-0002-4133-0757
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/144059
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