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

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Author(s)

    • 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
    • Watanabe Toshio
    • Institute of Development, Aging and Cancer, Graduate School of Life Sciences, 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

Abstract

SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the <i>trans</i>-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 <i>SMAP2</i> (–/–) 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>

Journal

  • Cell Structure and Function

    Cell Structure and Function 36(1), 83-95, 2011

    Japan Society for Cell Biology

Codes

  • NII Article ID (NAID)
    130004137566
  • Text Lang
    ENG
  • ISSN
    0386-7196
  • Data Source
    J-STAGE 
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