A SMAP Gene Family Encoding ARF GTPase-Activating Proteins and Its Implication in Membrane Trafficking

Kenji Tanabe, Shunsuke Kon, Nobuyuki Ichijo, Tomo Funaki, Waka Natsume, Toshio Watanabe, Masanobu Satake

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)


SMAP1 and SMAP2 proteins constitute a subfamily of the Arf-specific GTPase-activating proteins. Both SMAP proteins bind to clathrin heavy chains and are involved in the trafficking of clathrin-coated vesicles. In cells, SMAP1 regulates Arf6-dependent endocytosis of transferrin receptors from the coated pits of the plasma membrane, whereas SMAP2 regulates Arf1-dependent retrograde transport of TGN38 from the early endosome to the trans-Golgi network. The common and distinct features of SMAP1 and SMAP2 activity provide a valuable opportunity to examine the differential regulation of membrane trafficking by these two proteins. In this chapter, we describe several basic experimental procedures that have been used to study the regulation of membrane trafficking using SMAP proteins, including a GAP assay as well as procedures to study the transport of transferrin receptors and TGN38. In addition, a yeast two-hybrid system is described because of its utility in identifying novel molecules that interact with SMAP.

Original languageEnglish
Title of host publicationSmall GTPases in Disease, Part A
EditorsWilliam Balch, Alan Hall, Channing Der
Number of pages16
Publication statusPublished - 2008

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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