Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase.
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.
Biggs
W H
WH
Howard Hughes Medical Institute, University of California, Los Angeles 90024.
Zipursky
S L
SL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D003001:Cloning, Molecular; D004331:Drosophila melanogaster / Q000196:embryology / Q000201:enzymology*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D010766:Phosphorylation; D019000:Phosphotyrosine; D011494:Protein Kinases / Q000737:chemistry*; D016415:Sequence Alignment; D015398:Signal Transduction; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism
D009838:Oligodeoxyribonucleotides; D019000:Phosphotyrosine; D014443:Tyrosine; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases