Localization of SMAP2 to the TGN and its Function in the Regulation of TGN Protein Transport

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  • Funaki Tomo
    Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University
  • Kon Shunsuke
    Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University
  • Ronn Roger E.
    Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University
  • Henmi Yuji
    Graduate School of Medicine and Dentistry, Okayama University
  • Kobayashi Yuka
    Graduate School of Medicine and Dentistry, Okayama University
  • Watanabe Toshio
    Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University
  • Nakayama Keiko
    Graduate School of Medicine, Tohoku University
  • Tanabe Kenji
    Graduate School of Medicine and Dentistry, Okayama University
  • Satake Masanobu
    Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University

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SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-Golgi network (TGN) was verified as an additional site of SMAP2 localization based on its co-localization with various TGN-marker proteins. Mutation of specific stretches of basic amino acid residues abolished the TGN-localization of SMAP2. Over-expression of wild-type SMAP2, but not of the mutated SMAP2, inhibited the transport of vesicular stomatitis virus-G protein from the TGN to the plasma membrane. In contrast, this transport was enhanced in SMAP2 (–/–) cells characterized by increased levels of the activated form of Arf. SMAP2 therefore belongs to an ArfGAP subtype that resides on the TGN and functions as a negative regulator of vesicle budding from the organelle.<br>

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