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1.
Cell Rep ; 14(1): 11-21, 2016 Jan 05.
Article in English | MEDLINE | ID: mdl-26725111

ABSTRACT

Unveiling the molecular and cellular mechanisms underlying memory has been a challenge for the past few decades. Although synaptic plasticity is proven to be essential for memory formation, the significance of "single-cell memory" still remains elusive. Here, we exploited a primary culture system for the analysis of C. elegans neurons and show that a single thermosensory neuron has an ability to form, retain, and reset a temperature memory. Genetic and proteomic analyses found that the expression of the single-cell memory exhibits inter-individual variability, which is controlled by the evolutionarily conserved CaMKI/IV and Raf pathway. The variable responses of a sensory neuron influenced the neural activity of downstream interneurons, suggesting that modulation of the sensory neurons ultimately determines the behavioral output in C. elegans. Our results provide proof of single-cell memory and suggest that the individual differences in neural responses at the single-cell level can confer individuality.


Subject(s)
Caenorhabditis elegans/metabolism , Memory/physiology , Nerve Net/physiology , Neuronal Plasticity/physiology , Signal Transduction/physiology , Animals , Caenorhabditis elegans/genetics , Caenorhabditis elegans Proteins/metabolism , Calcium-Calmodulin-Dependent Protein Kinase Type 1/metabolism , Calcium-Calmodulin-Dependent Protein Kinase Type 4/metabolism , raf Kinases/metabolism
2.
Biochem Genet ; 41(5-6): 151-63, 2003 Jun.
Article in English | MEDLINE | ID: mdl-12834045

ABSTRACT

Phenol oxidase exists in Drosophila hemolymph as a prophenol oxidase, A1 and A3, that is activated in vivo with a native activating system, AMM-1, by limited proteolysis with time. The polypeptide in purified prophenol oxidase A3 has a molecular weight of approximately 77,000 Da. A PCR-based cDNA sequence coding A3 has 2501 bp encoding an open reading frame of 682 amino acid residues. The potential copper-binding sites, from Trp-196 to Tyr-245, and from Asn-366 to Phe-421, are highly homologous to the corresponding sites in other invertebrates. The availability of prophenol oxidase cDNA should be useful in revealing the biochemical differences between A1 and A3 isoforms in Drosophila melanogaster that are refractory or unable to activate prophenol oxidase.


Subject(s)
Catechol Oxidase/genetics , Catechol Oxidase/metabolism , DNA, Complementary/genetics , Drosophila melanogaster/enzymology , Enzyme Precursors/genetics , Enzyme Precursors/metabolism , Amino Acid Sequence , Animals , Base Sequence , Catechol Oxidase/isolation & purification , Drosophila melanogaster/genetics , Electrophoresis, Polyacrylamide Gel , Endopeptidases/pharmacology , Enzyme Activation/drug effects , Enzyme Precursors/isolation & purification , Isoenzymes/genetics , Isoenzymes/isolation & purification , Isoenzymes/metabolism , Molecular Sequence Data , Polymerase Chain Reaction , Sequence Alignment , Sequence Homology, Amino Acid
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