Publication Date:
1997-01-24
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sone, M -- Hoshino, M -- Suzuki, E -- Kuroda, S -- Kaibuchi, K -- Nakagoshi, H -- Saigo, K -- Nabeshima, Y -- Hama, C -- New York, N.Y. -- Science. 1997 Jan 24;275(5299):543-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, National Institute of Neuroscience (NIN), National Center of Neurology and Psychiatry (NCNP), Kodaira, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999801" target="_blank"〉PubMed〈/a〉
Keywords:
Actins/metabolism
;
Amino Acid Sequence
;
Animals
;
Axons/physiology
;
Cell Membrane/ultrastructure
;
Cytoskeleton/physiology/ultrastructure
;
DNA, Complementary/genetics
;
Drosophila/embryology/genetics/*metabolism
;
*Drosophila Proteins
;
Embryo, Nonmammalian/metabolism
;
GTP Phosphohydrolases/metabolism
;
GTP-Binding Proteins/genetics/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
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
