Several other transcription regulators are required for proper LTM including Adf-1 and Stat92E in Drosophila, and CCAAT/enhancer-binding protein, Zif268, AP-1, and NF-kB in mammals. The Notch signaling receptor has also been implicated in LTM. In addition to transcription, local control of translation, and proteases are as well involved in Drosophila LTM. Crammer, a protein required for LTM, has been shown to inhibit Cathepsin L, a protease that could be involved in lysosome function. A large collection of evidence indicates that mushroom bodies play a pivotal role in olfactory memory. The MBs form a bilaterally symmetrical structure in the central brain and consist of approximately 4,000 neurons called Kenyon cells. Three types of Kenyon cells project their axons ventrally to form the peduncle that splits into five lobes, two vertical and three median. The lobes are assumed to be the synaptic output region of the MBs. In addition, neurons of the lobes are targeted by multiple inputs. Many genes required for LTM have been shown to be expressed in the MBs, prompting us to analyze enhancertrap P lines showing Gal4 expression in the MBs to characterize new LTM mutants. In this report we identify debra, a gene involved in protein degradation by the lysosome, as being specifically required for LTM. We report here the identification of dbr as a new LTM mutant. We show that enhancer-trap P inserted nearby the dbr gene lead to Gal4-dependent expression in the MBs, a major center of olfactory memory. The MB247 driver used to affect dbr levels in our study leads to a specific expression in the MB a/b and c neurons, consistent with additional reports showing that these neurons are involved in aversive olfactory LTM. Several reports have shown that dbr is involved in various developmental processes. Importantly, the use of conditional silencing in our study reveals that the LTM-specific impairment observed is not caused by a developmental defect, demonstrating that dbr is physiologically involved in LTM Fingolimod processing. Dbr does not exhibit any obvious homology with known proteins, and its molecular function is unknown. Dbr has been shown to interact with the F-box protein Slimb, an ubiquitin ligase. In cooperation with Slimb, Dbr induces the polyubiquitination of phosphorylated Ci-155, a transcription factor that mediates Hedgehog signaling. Interestingly, similar to Dbr, Slimb has been implicated in LTM formation, thus pointing to a role for ubiquitination in LTM processing. These observations are reminiscent of a previous study showing that the highly conserved ubiquitin ligase Neuralized is involved in LTM. Neur is expressed in the adult MB a/b neurons and is a limiting factor for LTM formation: loss of one copy of neur gene results in significant LTM impairment whereas Neur overexpression results in a dose-dependent enhancement of LTM. In contrast, both dbr silencing and dbr overexpression in the adult MBs generate a LTM defect, showing that dbr levels must be precisely regulated to support normal LTM, a situation similar to previous reports describing LTM-specific mutants.