The Importance of Interaction with Membrane Lipids through the Pleckstrin Homology Domain of the Guanine Nucleotide Exchange Factor for Rho Family Small Guanosine Triphosphatase, FLJ00018

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  • Kimura Shinji
    Department of Biomolecular Science, Faculty of Engineering, Gifu University
  • Sato Katsuya
    The United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University
  • Banno Yoshiko
    Department of Cell Signaling, Graduate School of Medicine, Gifu University
  • Nagase Takahiro
    Kazusa DNA Research Institute
  • Ueda Hiroshi
    Department of Biomolecular Science, Faculty of Engineering, Gifu University The United Graduate School of Drug Discovery and Medical Information Sciences, Gifu University

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FLJ00018, a heterotrimeric guanosine 5′-triphosphate (GTP)-binding protein (G protein) Gβγ subunit-activated guanine nucleotide exchange factor for Rho family small GTPases, regulates cellular responses, including cell morphological changes and gene transcriptional regulation, and targets the cellular membranes. FLJ00018 contains a Dbl homology (DH) domain in addition to a pleckstrin homology (PH) domain. Here we show that the PH domain of FLJ00018 is required for FLJ00018-induced, serum response element-dependent gene transcription. Although the PH domain of KIAA1415/P-Rex1, another Gβγ subunit-activated guanine nucleotide exchange factor for Rho family small GTPases, binds to phosphatidylinositol 3,4,5-triphosphate and phosphatidylinositol 3,4-bisphosphate, the PH domain of FLJ00018 binds to polyphosphoinositides including phosphatidylinositol 4,5-bisphosphate, and phosphatidic acid. These results suggest that FLJ00018 is targeted via its PH domain to cellular membranes.

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