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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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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| uniprot:name |
Proc. Natl. Acad. Sci. U.S.A.
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| uniprot:erratum | |
| uniprot:author |
Biggs W.H. III,
Zipursky S.L.
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| uniprot:date |
1992
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| uniprot:pages |
6295-6299
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| uniprot:title |
Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase.
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| uniprot:volume |
89
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| dc-term:identifier |
doi:10.1073/pnas.89.14.6295
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