Reference - Detail
|Author||Sone M, Hoshino M, Suzuki E, Kuroda S, Kaibuchi K, Nakagoshi H, Saigo K, Nabeshima Y, Hama C.|
|Title||Still life, a protein in synaptic terminals of Drosophila homologous to GDP-GTP exchangers.|
The morphology of axon terminals changes with differentiation into mature synapses. A molecule that might regulate this process was identified by a screen of Drosophila mutants for abnormal motor activities. The still life (sif) gene encodes a protein homologous to guanine nucleotide exchange factors, which convert Rho-like guanosine triphosphatases (GTPases) from a guanosine diphosphate-bound inactive state to a guanosine triphosphate-bound active state. The SIF proteins are found adjacent to the plasma membrane of synaptic terminals. Expression of a truncated SIF protein resulted in defects in neuronal morphology and induced membrane ruffling with altered actin localization in human KB cells. Thus, SIF proteins may regulate synaptic differentiation through the organization of the actin cytoskeleton by activating Rho-like GTPases.
|MeSH||Actins / metabolism Amino Acid Sequence Animals Axons / physiology Cell Membrane / ultrastructure Cytoskeleton / physiology Cytoskeleton / ultrastructure DNA, Complementary / genetics Drosophila / embryology Drosophila / genetics Drosophila / metabolism* Drosophila Proteins* Embryo, Nonmammalian / metabolism GTP Phosphohydrolases / metabolism GTP-Binding Proteins / genetics GTP-Binding Proteins / metabolism Gene Expression Genes, Insect Guanine Nucleotide Exchange Factors* Humans In Situ Hybridization KB Cells Molecular Sequence Data Movement Mutation Neuromuscular Junction / metabolism Presynaptic Terminals / metabolism* Signal Transduction rac GTP-Binding Proteins*|
|WOS Category||BIOCHEMISTRY & MOLECULAR BIOLOGY|