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Primary Structure, Expression, and Signal-Dependent Tyrosine Phosphorylation of a Drosophila Homolog of Extracellular Signal-Regulated Kinase

William H. Biggs III and S. Lawrence Zipursky
Proceedings of the National Academy of Sciences of the United States of America
Vol. 89, No. 14 (Jul. 15, 1992), pp. 6295-6299
Stable URL: http://www.jstor.org/stable/2359996
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Primary Structure, Expression, and Signal-Dependent Tyrosine Phosphorylation of a Drosophila Homolog of Extracellular Signal-Regulated Kinase
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Abstract

The extracellular signal-regulated kinases (ERKs) comprise a class of protein-serine/threonine kinases that are activated in response to a wide variety of extracellular signals transduced via receptor tyrosine kinases. Activation of the ERKs requires both threonine and tyrosine phosphorylation suggestive of a key role in mediating intracellular events in response to extracellular cues. To critically assess the role of ERKs in intracellular signaling, a genetically tractable receptor tyrosine kinase system would be invaluable. In this paper we report the identification of a Drosophila homolog of ERK1 and -2, designated DmERK-A. DmERK-A is 80% identical to rat ERK1 and -2 and is rapidly phosphorylated on tyrosine in response to an extracellular signal activating a receptor tyrosine kinase. Biochemical and histological studies reveal its expression in the eye imaginal disc. These studies provide a first step in a genetic analysis of ERK function.

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