Signal Transduction of Heterotrimeric G Protein Goα in Glycosphingolipid Microdomains

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  • 三量体Gタンパク質Goαの糖脂質ミクロドメイン
  • 三量体Gタンパク質Goαの糖脂質ミクロドメインにおけるシグナル伝達
  • サンリョウタイ Gタンパクシツ Goa ノ トウ シシツ ミクロドメイン ニ オケル シグナル デンタツ

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Abstract

The association of gangliosides with specific proteins in the central nervous system was examined by co-immunoprecipitation with an anti-ganglioside antibody. The monoclonal antibody to the ganglioside GD3 immunoprecipitated the α-subunit of a heterotrimeric G protein, Go (Goα) from the rat cerebellum. Using sucrose density gradient analysis, Goα, but not Gβγ, was observed in detergent-resistant membrane (DRM) raft fractions, after the addition of GTPγS. On the other hand, both Goα and Gβγwere excluded from the DRM raft fractions in the presence of GDPβS. Only Goα was observed in the DRM fractions from the cerebellum on postnatal day 7, but not from that in adult. After pertussis toxin treatment, Goα was not observed in the DRM fractions, even from the cerebellum on postnatal day 7. These results indicate the activation-dependent translocation of Goα into the DRM rafts. Furthermore, treatment with stromal cell-derived factor-1α stimulated [35S]GTPγS binding to Goα, and caused Goα translocation to the DRM fractions, leading to growth cone collapse of cerebellar granule neurons. These results demonstrate involvement of signal - dependent Goα translocation to DRM in the growth cone behavior of cerebellar granule neurons.

Journal

  • MEMBRANE

    MEMBRANE 37 (4), 168-173, 2012

    THE MEMBRANE SOCIETY OF JAPAN

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