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Vol. 17, Issue 6, 2592-2603, June 2006

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SMAP2, a Novel ARF GTPase-activating Protein, Interacts with Clathrin and Clathrin Assembly Protein and Functions on the AP-1–positive Early Endosome/Trans-Golgi Network

Department of Molecular Immunology, Institute of Development, Aging, and Cancer, Tohoku University, Sendai 980-8575, Japan

Submitted October 3, 2005; Revised March 20, 2006; Accepted March 20, 2006
Monitoring Editor: Suzanne Pfeffer

We recently reported that SMAP1, a GTPase-activating protein (GAP) for Arf6, directly interacts with clathrin and regulates the clathrin-dependent endocytosis of transferrin receptors from the plasma membrane. Here, we identified a SMAP1 homologue that we named SMAP2. Like SMAP1, SMAP2 exhibits GAP activity and interacts with clathrin heavy chain (CHC). Furthermore, we show that SMAP2 interacts with the clathrin assembly protein CALM. Unlike SMAP1, however, SMAP2 appears to be a regulator of Arf1 in vivo, because cells transfected with a GAP-negative SMAP2 mutant were resistant to brefeldin A. SMAP2 colocalized with the adaptor proteins for clathrin AP-1 and EpsinR on the early endosomes/trans-Golgi-network (TGN). Moreover, overexpression of SMAP2 delayed the accumulation of TGN38/46 molecule on the TGN. This suggests that SMAP2 functions in the retrograde, early endosome-to-TGN pathway in a clathrin- and AP-1–dependent manner. Thus, the SMAP gene family constitutes an important ArfGAP subfamily, with each SMAP member exerting both common and distinct functions in vesicle trafficking.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

* These authors contributed equally to this work.

Address correspondence to: Masanobu Satake ( satake{at}idac.tohoku.ac.jp)

Abbreviations used: Arf, ADP-ribosylation factor; BFA, brefeldin A; CHC, clathrin heavy chain; GAP, GTPase-activating protein; GEF, guanine-nucleotide exchange factor; GST, glutathione S-transferase; HA, influenza hemagglutinin; TGN, trans-Golgi network.

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