Still life, a protein in synaptic terminals of Drosophila homologous to GDP-GTP exchangers

Masaki Sone, Mikio Hoshino, Emiko Suzuki, Shinya Kuroda, Kozo Kaibuchi, Hideki Nakagoshi, Kaoru Saigo, Yo Ichi Nabeshima, Chihiro Hama

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77 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)543-547
Number of pages5
JournalScience
Volume275
Issue number5299
DOIs
Publication statusPublished - Jan 24 1997
Externally publishedYes

ASJC Scopus subject areas

  • General

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    Sone, M., Hoshino, M., Suzuki, E., Kuroda, S., Kaibuchi, K., Nakagoshi, H., Saigo, K., Nabeshima, Y. I., & Hama, C. (1997). Still life, a protein in synaptic terminals of Drosophila homologous to GDP-GTP exchangers. Science, 275(5299), 543-547. https://doi.org/10.1126/science.275.5299.543