田邊　賢司    Department   Research Institutes and Facilities, Research Institutes and Facilities    Position   Associate Professor
Article types	Original article
Language	English
Peer review	Peer reviewed
Title	The carboxy-terminal region of SMAP2 directs subcellular localization as well as Arf protein specificity.
Journal	Formal name：Biochemical and biophysical research communications
Volume, Issue, Page	404,pp.661-666
Author and coauthor	Sakakura, Ikuko Tanabe, Kenji Nouki, Natsumi Suzuki, Mai Satake, Masanobu Watanabe, Toshio
Authorship	Lead author
Publication date	2011
Summary	Small G proteins play a central role in theorganization of secretory and endocytotic pathways. The recruitment of some effectors, including vesicle coat proteins, is mediated by the ADP-ribosylation factor (Arf) family. Arf proteins have distinct subcellular localizations. ArfGAPs (Arf GTPase-activating proteins) regulate Arf GTPase activity. Thus, each ArfGAP is distinctly localized to allow it to maintain a specific interaction with its target Arf(s). However, the domains that regulate the subcellular localization of ArfGAPs and the way in which these subcellular localizations affect the target specificities of ArfGAPs remain unclear. Recently, we identified two novel ArfGAPs, SMAP1 (Small ArfGAP protein 1) and SMAP2. In the current study, we identified sequences in the carboxy-terminal region of SMAP2 that are critical for its specific subcellular localization and its specificity for Arf proteins.