fm1-43 has been researched along with Eye-Abnormalities* in 2 studies
2 other study(ies) available for fm1-43 and Eye-Abnormalities
| Article | Year |
|---|---|
Tweek, an evolutionarily conserved protein, is required for synaptic vesicle recycling.
Synaptic vesicle endocytosis is critical for maintaining synaptic communication during intense stimulation. Here we describe Tweek, a conserved protein that is required for synaptic vesicle recycling. tweek mutants show reduced FM1-43 uptake, cannot maintain release during intense stimulation, and harbor larger than normal synaptic vesicles, implicating it in vesicle recycling at the synapse. Interestingly, the levels of a fluorescent PI(4,5)P(2) reporter are reduced at tweek mutant synapses, and the probe is aberrantly localized during stimulation. In addition, various endocytic adaptors known to bind PI(4,5)P(2) are mislocalized and the defects in FM1-43 dye uptake and adaptor localization are partially suppressed by removing one copy of the phosphoinositide phosphatase synaptojanin, suggesting a role for Tweek in maintaining proper phosphoinositide levels at synapses. Our data implicate Tweek in regulating synaptic vesicle recycling via an action mediated at least in part by the regulation of PI(4,5)P(2) levels or availability at the synapse. Topics: Animals; Blotting, Western; Diptera; DNA, Complementary; Drosophila Proteins; Endocytosis; Eye Abnormalities; Immunohistochemistry; Microscopy, Electron, Transmission; Molecular Sequence Data; Mutation; Nerve Tissue Proteins; Neurons; Phosphatidylinositol Phosphates; Pyridinium Compounds; Quaternary Ammonium Compounds; Reverse Transcriptase Polymerase Chain Reaction; Synapses; Synaptic Transmission; Synaptic Vesicles | 2009 |
The v-ATPase V0 subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila.
The V(0) complex forms the proteolipid pore of an ATPase that acidifies vesicles. In addition, an independent function in membrane fusion has been proposed largely based on yeast vacuolar fusion experiments. We have isolated mutations in the largest V(0) component vha100-1 in flies in an unbiased genetic screen for synaptic malfunction. The protein is only required in neurons, colocalizes with markers for synaptic vesicles as well as active zones, and interacts with t-SNAREs. Loss of vha100-1 leads to vesicle accumulation in synaptic terminals, suggesting a deficit in release. The amplitude of spontaneous release events and release with hypertonic stimulation indicate normal levels of neurotransmitter loading, yet mutant embryos display severe defects in evoked synaptic transmission and FM1-43 uptake. Our data suggest that Vha100-1 functions downstream of SNAREs in synaptic vesicle fusion. Topics: Animals; Drosophila melanogaster; Embryo, Nonmammalian; Exocytosis; Eye Abnormalities; Hypertonic Solutions; Membrane Fusion; Microscopy, Electron; Mutation; Photoreceptor Cells, Invertebrate; Protein Subunits; Pyridinium Compounds; Quaternary Ammonium Compounds; SNARE Proteins; Synaptic Membranes; Synaptic Transmission; Synaptic Vesicles; Vacuolar Proton-Translocating ATPases; Vesicular Transport Proteins | 2005 |