Isolation and characterization of a Drosophila homologue of mitogen-activated protein kinase phosphatase-3 which has a high substrate specificity towards extracellular-signal-regulated kinase

Sun Hong Kim, Hyung Bae Kwon, Yong Sik Kim, Ji Hwan Ryu, Kyung Sub Kim, Yongho Ahn, Won Jae Lee, Kang-Yell Choi

Research output: Contribution to journalArticle

28 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)143-151
Number of pages9
JournalBiochemical Journal
Volume361
Issue number1
DOIs
Publication statusPublished - 2002 Jan 1

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Dual Specificity Phosphatase 6
Extracellular Signal-Regulated MAP Kinases
Substrate Specificity
Drosophila
Gene expression
Substrates
Complementary DNA
Mitogen-Activated Protein Kinase Phosphatases
Amino Acids
JNK Mitogen-Activated Protein Kinases
Expressed Sequence Tags
Molecular mass
Gene Library
Gene Expression
Phosphoric Monoester Hydrolases
Escherichia coli
Tyrosine
Epitopes
Reporter Genes
Amino Acid Sequence

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kim, Sun Hong ; Kwon, Hyung Bae ; Kim, Yong Sik ; Ryu, Ji Hwan ; Kim, Kyung Sub ; Ahn, Yongho ; Lee, Won Jae ; Choi, Kang-Yell. / Isolation and characterization of a Drosophila homologue of mitogen-activated protein kinase phosphatase-3 which has a high substrate specificity towards extracellular-signal-regulated kinase. In: Biochemical Journal. 2002 ; Vol. 361, No. 1. pp. 143-151.
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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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Isolation and characterization of a Drosophila homologue of mitogen-activated protein kinase phosphatase-3 which has a high substrate specificity towards extracellular-signal-regulated kinase. / Kim, Sun Hong; Kwon, Hyung Bae; Kim, Yong Sik; Ryu, Ji Hwan; Kim, Kyung Sub; Ahn, Yongho; Lee, Won Jae; Choi, Kang-Yell.

In: Biochemical Journal, Vol. 361, No. 1, 01.01.2002, p. 143-151.

Research output: Contribution to journalArticle

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