| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1930716 | Biochemical and Biophysical Research Communications | 2011 | 6 Pages |
Small G proteins play a central role in the organization 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.
Research highlights► SMAP2, newly identified ArfGAP, functions as an Arf1-specific GAP. ► The domains that regulate the subcellular localization of SMAP2 remain unknown. ► The carboxy-terminal region of SMAP2 directs subcellular localization. ► These sequences are also crucial for the specificity of SMAP2 for Arf proteins.
