Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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Amino Acid Sequence
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Animals
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Axons / physiology
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Cell Membrane / ultrastructure
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Cytoskeleton / physiology
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Cytoskeleton / ultrastructure
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DNA, Complementary / genetics
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Drosophila / embryology
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Drosophila / genetics
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Drosophila / metabolism*
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Drosophila Proteins*
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Embryo, Nonmammalian / metabolism
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GTP Phosphohydrolases / metabolism
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GTP-Binding Proteins / genetics
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GTP-Binding Proteins / metabolism
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Gene Expression
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Genes, Insect
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Guanine Nucleotide Exchange Factors*
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Humans
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In Situ Hybridization
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KB Cells
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Molecular Sequence Data
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Movement
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Mutation
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Neuromuscular Junction / metabolism
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Presynaptic Terminals / metabolism*
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Signal Transduction
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rac GTP-Binding Proteins*
Substances
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Actins
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Cdc42 protein, Drosophila
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DNA, Complementary
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Drosophila Proteins
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Guanine Nucleotide Exchange Factors
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Rac1 protein, Drosophila
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sif protein, Drosophila
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GTP Phosphohydrolases
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GTP-Binding Proteins
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rac GTP-Binding Proteins
Associated data
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GENBANK/D86546
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GENBANK/D86547