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J. Biol. Chem., Vol. 275, Issue 27, 20588-20596, July 7, 2000
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From the Department of Biology, University of Virginia,
Charlottesville, Virginia 22903
We identified a unique type II
cAMP-dependent protein kinase regulatory subunit (PKA-RII)
gene in Drosophila melanogaster and a severely hypomorphic
if not null mutation, pka-RIIEP(2)2162.
Extracts from pka- RIIEP(2)2162 flies selectively
lack RII-specific autophosphorylation activity and show significantly
reduced cAMP binding activity, attributable to the loss of functional
PKA-RII. pka-RIIEP(2)2162 shows 2-fold increased
basal PKA activity and ~40% of normal cAMP-inducible PKA activity.
pka-RIIEP(2)2162 is fully viable but displays
abnormalities of ovarian development and multiple behavioral phenotypes
including arrhythmic circadian locomotor activity, decreased
sensitivity to ethanol and cocaine, and a lack of sensitization to
repeated cocaine exposures. These findings implicate type II PKA
activity in these processes in Drosophila and imply a
common role for PKA signaling in regulating responsiveness to cocaine
and alcohol.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF274008.
Type II cAMP-dependent Protein Kinase-deficient
Drosophila Are Viable but Show Developmental, Circadian,
and Drug Response Phenotypes*
*
This work was supported by National Institutes of Health
Grant GM/DA 27318 (to J. H.) and National Science Foundation Grant IBN-9723350 (to C. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biology,
Gilmer Hall, University of Virginia, Charlottesville, VA 22903. Tel.:
804-982-5608; Fax: 804-982-5626; E-mail: jh6u@virginia.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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