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. 2011;36(1):83-95.
doi: 10.1247/csf.10022. Epub 2011 Feb 26.

Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport

Tomo Funaki  1 , Shunsuke Kon, Roger E Ronn, Yuji Henmi, Yuka Kobayashi, Toshio Watanabe, Keiko Nakayama, Kenji Tanabe, Masanobu Satake
Affiliations
Free article

Localization of SMAP2 to the TGN and its function in the regulation of TGN protein transport

Tomo Funaki et al. Cell Struct Funct. 2011.
Free article

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.

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