The Fickle mutatation of a cytoplasmic tyrosine kinase effects sensitization but not dishabituation in Drosophila melanogaster

Asztalos, Z., Baba, K., Yamamoto, D., Tully, T. (January 2007) The Fickle mutatation of a cytoplasmic tyrosine kinase effects sensitization but not dishabituation in Drosophila melanogaster. J Neurogenet, 21 (1). pp. 59-71. ISSN 0167-7063 (Print)

URL: https://www.ncbi.nlm.nih.gov/pubmed/17464798
DOI: 10.1080/01677060701249488

Abstract

fickle is a P-element mutation identified from a screen for defects in courtship behavior and disrupts the fly homolog of Bruton's tyrosine kinase (Btk) gene (Baba et al., 1999). Here, we show that habituation of the olfactory jump reflex also is defective in fickle. Unlike, the prototypical memory mutants, rutabaga and dunce, which habituate more slowly than normal, fickle flies habituate faster than normal. fickle's faster-than-normal response decrement did not appear to be due to sensorimotor fatigue, and dishabituation of the jump response was normal. Based on a long-standing "two opponent process" theory of habituation, these data suggested that behavioral sensitization might be defective in fickle. To test this hypothesis, we designed a olfactory sensitization procedure, using the same stimuli to habituate (odor) and dishabituate (vortexing) flies. Mutant flies failed to show any sensitization with this procedure. Our study reveals a "genetic dissection" of sensitization and dishabituation and, for the first time, provides a biological confirmation of the two opponent process theory of habituation.

Item Type: Paper
Uncontrolled Keywords: behavioral Drosophila enzymatic mutant olfactory jump reflex sensitization LONG-TERM POTENTIATION APLYSIA SENSORY NEURONS PRESYNAPTIC FACILITATION MUTANT MICE MEMORY
Subjects: organism description > animal > insect > Drosophila
organism description > animal behavior > habituation
organism description > animal behavior > olfactory jump reflex
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
CSHL Authors:
Communities: CSHL labs > Tully lab
Depositing User: CSHL Librarian
Date: January 2007
Date Deposited: 02 Dec 2011 16:52
Last Modified: 21 Mar 2018 13:52
PMCID: PMC2409174
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22963

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