Abstract
Background: Learning and memory are extremely complex and dynamic processes. Proteins that participate in memory formation are strictly regulated by various pathways and may require protein synthesis and/or posttranslational modifications. To examine the formation of memory, Drosophila was genetically engineered with the mutated memory-related gene, Amn X8 , which induces normal learning and memory behavior within the first 30 min of training. However, the process through which learning occurred could not be retained after the 30 min of training, indicating that these mutants possessed deficits in middle-term memory. A proteomics platform based on two-dimensional differential gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry was employed to examine the head proteome alterations between the wild-type 2u strain and the memory-deficient mutant Amn X8 strain. Results: The results indicated that 30 differentially expressed head proteins that mainly function in metabolic pathways and cell structure/cytoskeleton proteins were involved in memory formation. A bioinformatics analysis demonstrated that mitochondrial proteins had critical roles in modulating this process. Conclusions: This is the first study of a comparative head proteomics analysis of a memory mutant strain and a normal control fruit fly strain. The fundamental proteomics analysis provides potential candidates for further elucidation of the biological mechanism of the memory formation process in Drosophila. © 2013 Lee et al.