Localization of SMAP2 to the TGN and its Function in the Regulation of TGN Protein Transport

Cell Structure and Function

Keiko Nakayama³  Yuji Henmi²  Tomo Funaki¹  Toshio Watanabe¹  Roger E. Ronn¹  Yuka Kobayashi²  Shunsuke Kon¹  Masanobu Satake¹  Kenji Tanabe² 

[1] Institute of Development, Aging and Cancer, Graduate School of Life Sciences, Tohoku University;Graduate School of Medicine and Dentistry, Okayama University;Graduate School of Medicine, Tohoku University

关键词: Arf GTPase;    clathrin-coated vesicles;    gene targeting;    membrane traffic;    trans-Golgi network;   

DOI  :  10.1247/csf.10022

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(38)Cited-By(6)Supplementary materials(5)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.

【 授权许可】

Unknown