The cyclic AMP phosphodiesterase encoded by the Drosophila dunce gene is concentrated in the mushroom body neuropil.
Drosophila dunce (dnc) flies are defective in learning and memory as a result of lesions in the gene that codes for a cAMP-specific phosphodiesterase (PDE). Antibodies to the dnc PDE showed that the most intensely stained regions in the adult brain were the mushroom body neuropil--areas previously implicated in learning and memory. In situ hybridization demonstrated that dnc RNA was enriched in the mushroom body perikarya. The mushroom bodies of third instar larval brains were also stained intensely by the antibody, suggesting that the dnc PDE plays an important role in these neurons throughout their development. The role of the dnc PDE in mushroom body physiology is discussed, and a circuit model describing a possible role of the mushroom bodies in mediating olfactory learning and memory is presented.
Nighorn
A
A
Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.
Healy
M J
MJ
Davis
R L
RL
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000235:genetics* / Q000502:physiology; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000166:cytology / Q000196:embryology / Q000201:enzymology; D004247:DNA / Q000235:genetics; D015342:DNA Probes; D004330:Drosophila / Q000235:genetics* / Q000378:metabolism / Q000502:physiology; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000201:enzymology; D005815:Genetic Code; D007150:Immunohistochemistry / Q000379:methods; D007858:Learning / Q000502:physiology; D008568:Memory / Q000502:physiology; D008969:Molecular Sequence Data; D009154:Mutation; D009457:Neuroglia / Q000166:cytology / Q000201:enzymology*; D009474:Neurons / Q000166:cytology / Q000201:enzymology*; D009693:Nucleic Acid Hybridization; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D013909:Thorax / Q000166:cytology / Q000201:enzymology
D015342:DNA Probes; D012333:RNA, Messenger; D004247:DNA; D015105:3',5'-Cyclic-AMP Phosphodiesterases