Identification of a protein phosphorylated by cAMP-dependent protein kinase in drosophila brain.
In the present study, we examined the effects of reagents that elevate cAMP concentration on protein phosphorylation in Drosophila brain cells. Application of forskolin or dopamine to brain cells that were prelabeled with (32)Pi enhanced phosphorylation of a 25-kDa protein (p25a). To identify p25a, we isolated the protein, and partial amino acid sequences were analyzed. Database searches showed that p25a is a J-domain protein, dJDP that contains the J-domain found in the DnaJ (heat shock protein 40) family of molecular chaperones.
Inoue
H
H
School of Human Sciences, Waseda University, 2-579-15 Mikajima, Tokorozawa 359, Japan. hiroko@human.waseda.ac.jp
Chikaoka
Y
Y
Takahashi
M
M
Yoshioka
T
T
D000818:Animals; D001921:Brain / Q000187:drug effects / Q000378:metabolism*; D005576:Colforsin / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism*; D004298:Dopamine / Q000494:pharmacology; D004330:Drosophila / Q000378:metabolism*; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000235:genetics; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D017434:Protein Structure, Tertiary
D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D009419:Nerve Tissue Proteins; D005576:Colforsin; D017868:Cyclic AMP-Dependent Protein Kinases; D004298:Dopamine