
doi: 10.1002/arch.10012
pmid: 11816025
AbstractMutations in the canoe locus of Drosophila lead to failure in the dorsal closure of the embryonic epidermis and pattern formation defects in imaginal eyes and wings. In the wing, the canoe mutants develop extra veins when they are heterozygous for shaggy, a mutation in the locus encoding the glycogen synthase kinase 3β (Gsk3β), which has been known to phosphorylate the Armadillo protein. Although Canoe has a putative target sequence for phosphorylation by Gsk3β similar to that found in Armadillo, in vitro experiments indicate that Canoe is not phosphorylated by Gsk3β. Instead, Canoe is demonstrated to be a good substrate of Cdc2 and Cdk5 kinases. Thus, Cdc2 and Cdk5 kinases are the potential regulators of the function of Canoe in morphogenesis. Arch. Insect Biochem. Physiol. 49:102–107, 2002. © 2002 Wiley‐Liss, Inc.
Armadillo Domain Proteins, Binding Sites, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Molecular Sequence Data, Glycogen Synthase Kinases, Cyclin-Dependent Kinase 5, Protein Serine-Threonine Kinases, Cyclin-Dependent Kinases, Substrate Specificity, Glycogen Synthase Kinase 3, Drosophila melanogaster, CDC2 Protein Kinase, Calcium-Calmodulin-Dependent Protein Kinases, Animals, Drosophila Proteins, Insect Proteins, Cattle, Amino Acid Sequence, Phosphorylation
Armadillo Domain Proteins, Binding Sites, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Molecular Sequence Data, Glycogen Synthase Kinases, Cyclin-Dependent Kinase 5, Protein Serine-Threonine Kinases, Cyclin-Dependent Kinases, Substrate Specificity, Glycogen Synthase Kinase 3, Drosophila melanogaster, CDC2 Protein Kinase, Calcium-Calmodulin-Dependent Protein Kinases, Animals, Drosophila Proteins, Insect Proteins, Cattle, Amino Acid Sequence, Phosphorylation
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