Molecular cloning and characterization of a Drosophila p38 mitogen- activated protein kinase

Sung Jun Han, Kang-Yell Choi, Paul T. Brey, Won Jae Lee

Research output: Contribution to journalArticle

84 Citations (Scopus)

Abstract

A mitogen-activated protein kinase (MAPK) has been cloned and sequenced from a Drosophila neoplasmic l(2)mbn cell line. The cDNA sequence analysis showed that this Drosophila kinase is a homologue of mammalian p38 MAPK and the yeast HOG1 gene and thus was referred to as Dp38. A distinguishing feature of all MAPKs is the conserved sequence TGY in the activation domain. Dp38 was rapidly tyrosine 186-phosphorylated in response to osmotic stress, heat shock, serum starvation, and H2O2 in Drosophila l(2)mbn and Schneider cell lines. However, unlike mammalian p38 MAPK, the addition of lipopolysaccharide (LPS) did not significantly affect the phosphorylation of Dp38 in the LPS-responsive l(2)mbn cell line. Following osmotic stress, tyrosine 186-phosphorylated forms of Dp38 MAPK were detected exclusively in nuclear regions of Schneider cells. Yeast complementation studies demonstrated that the Saccharomyces cerevisiae HOG1 mutant strain JBY10 (hog1-Δ1) was functionally complemented by Dp38 cDNA in hyperosmolar medium. These findings demonstrate that similar osmotic stress-responsive signal transduction pathways are conserved in yeast, Drosophila, and mammalian cells, whereas LPS signal transduction pathways appear to be different.

Original languageEnglish
Pages (from-to)369-374
Number of pages6
JournalJournal of Biological Chemistry
Volume273
Issue number1
DOIs
Publication statusPublished - 1998 Jan 2

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Cloning
Molecular Cloning
p38 Mitogen-Activated Protein Kinases
Yeast
Drosophila
Cells
Lipopolysaccharides
Signal transduction
Yeasts
Osmotic Pressure
Mitogen-Activated Protein Kinases
Cell Line
Tyrosine
Signal Transduction
Complementary DNA
Osmoregulation
Phosphorylation
Conserved Sequence
Starvation
Sequence Analysis

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Molecular cloning and characterization of a Drosophila p38 mitogen- activated protein kinase",
abstract = "A mitogen-activated protein kinase (MAPK) has been cloned and sequenced from a Drosophila neoplasmic l(2)mbn cell line. The cDNA sequence analysis showed that this Drosophila kinase is a homologue of mammalian p38 MAPK and the yeast HOG1 gene and thus was referred to as Dp38. A distinguishing feature of all MAPKs is the conserved sequence TGY in the activation domain. Dp38 was rapidly tyrosine 186-phosphorylated in response to osmotic stress, heat shock, serum starvation, and H2O2 in Drosophila l(2)mbn and Schneider cell lines. However, unlike mammalian p38 MAPK, the addition of lipopolysaccharide (LPS) did not significantly affect the phosphorylation of Dp38 in the LPS-responsive l(2)mbn cell line. Following osmotic stress, tyrosine 186-phosphorylated forms of Dp38 MAPK were detected exclusively in nuclear regions of Schneider cells. Yeast complementation studies demonstrated that the Saccharomyces cerevisiae HOG1 mutant strain JBY10 (hog1-Δ1) was functionally complemented by Dp38 cDNA in hyperosmolar medium. These findings demonstrate that similar osmotic stress-responsive signal transduction pathways are conserved in yeast, Drosophila, and mammalian cells, whereas LPS signal transduction pathways appear to be different.",
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Molecular cloning and characterization of a Drosophila p38 mitogen- activated protein kinase. / Han, Sung Jun; Choi, Kang-Yell; Brey, Paul T.; Lee, Won Jae.

In: Journal of Biological Chemistry, Vol. 273, No. 1, 02.01.1998, p. 369-374.

Research output: Contribution to journalArticle

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