The crystal structure of the TBC domain of the Drosophila ortholog Skywalker revealing an unanticipated cationic pocket conserved among TBC1D24 homologs. Cocrystallization and biochemistry showed that this pocket binds phosphoinositides phosphorylated at the 4 and 5 positions. The most prevalent patient mutations affect the phosphoinositide-binding pocket and inhibit lipid binding.
this paper studies Drosophila melanogaster lacking active TBC1D24/Skywalker (Sky) a protein that in humans causes severe neurodegeneration epilepsy and DOOR (deafness onychdystrophy osteodystrophy and mental retardation) syndrome and identify endosome-to-lysosome trafficking as a mechanism for degradation of synaptic vesicle-associated proteins.
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