Abstract
SMAP2 is an Arf GTPase-activating protein that is located and functions on early endosome membranes. In the present study, the trans-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 SMAP2 (-/-) 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. © 2011 by Japan Society for Cell Biology.
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Funaki, T., Kon, S., Ronn, R. E., Henmi, Y., Kobayashi, Y., Watanabe, T., … Satake, M. (2011). Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport. Cell Structure and Function, 36(1), 83–95. https://doi.org/10.1247/csf.10022
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