Project description:Proteins co-purifying with recombinantly purified and N-terminally GFP-3C-tagged CTCF N-terminus (amino acids 1-293) produced in bacteria were identified by incubating the tagged bait with soluble nuclear protein extracts from 0-12h hour-old wildtype (OregonR strain) Drosophila melanogaster embryos.
Project description:Drosophila preblastoderm embryo extract assisted chromatin assembly with or without 16mer DNA mimic. Pull down of chromatin fiber to reveal chromatin binders in the system.
Project description:We have used ChIP followed by high throughput sequencing to profile the genome-wide recruitment of wildtype Groucho (Gro) at high resolution in BG3 Drosophila cells.
Project description:To clarify the role of Wdr92, and R2TP, in motile cilium formation, we explored its function in Drosophila. We show that Drosophila Wdr92 is a cytoplasmic protein exclusively expressed in motile ciliated cells and is required exclusively for ciliary/flagellar motility. The major effect of its mutation is loss of dynein arms from the axonemes of sensory neuron cilia and sperm flagella. We confirm that Drosophila Wdr92 interacts with R2TP and that R2TP depletion also impairs dynein arm formation. We provide proteomic evidence that Wdr92 is associated especially with heavy chain assembly and propose that it acts as a specificity factor to bring axonemal dynein clients to the R2TP/HSP90 complex. Thus, Wdr92 is a new dynein assembly factor and it strongly reinforces the critical role of HSP90 and co-chaperones in dynein assembly.
Project description:Neuroligins are transmembrane cell adhesion proteins well-known for their genetic links to autism spectrum disorders. Neuroligins can function by regulating the actin cytoskeleton, however the factors and mechanisms involved are still largely unknown. Here, using the Drosophila neuromuscular junction as a model, we reveal that F-Actin assembly at the Drosophila NMJ is controlled through Cofilin signaling mediated by an interaction between DNlg2 and RACK1, factors not previously known to work together. The deletion of DNlg2 displays disrupted RACK1-Cofilin signaling pathway with diminished actin cytoskeleton proteo-stasis at the terminal of the NMJ, aberrant NMJ structure, reduced synaptic transmission, and abnormal locomotion at the third-instar larval stage. Overexpression of wildtype and activated Cofilin in muscles are sufficient to rescue the morphological and physiological defects in dnlg2 mutants, while inactivated Cofilin is not. Since the DNlg2 paralog DNlg1 is known to regulate F-actin assembly mainly via a specific interaction with WAVE complex, our present work suggests that the orchestration of F-actin by Neuroligins is a highly dynamic and complex process critical for neural connectivity.
