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Arfaptin‐1 Negatively Regulates Arl1‐mediated Retrograde Transport
Author(s) -
Yu ChiaJung,
Huang LienHung,
Lee WeiChung,
You ShuTing,
Cheng ChiaChen
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.lb179
Subject(s) - rab , golgi apparatus , gene knockdown , transport protein , endosome , axoplasmic transport , protein subunit , vesicular transport protein , intracellular , chemistry , small gtpase , shiga toxin , microbiology and biotechnology , biology , biochemistry , gtpase , gene , vesicle , signal transduction , membrane , cell , virulence
Thesmall GTPase Arf‐like protein 1 (Arl1) is well known for its role in intracellular vesicular transport at the trans ‐Golgi network (TGN). In this study, we used differential affinity chromatography combined with mass spectrometry to identify Arf‐interacting protein 1b (arfaptin‐1b) as an Arl1‐interacting protein and characterized a novelfunction for arfaptin‐1 (including the arfaptin‐1a and 1b isoforms) in Arl1‐mediated retrograde transport. Using a Shiga‐toxin subunit B (STxB) transportation assay, we demonstrated that knockdown of arfaptin‐1 accelerated the retrograde transport of STxB from the endosome to the Golgi apparatus, whereas Arl1 knockdown inhibited STxB transport compared with control cells. Arfaptin‐1 overexpression, but not an Arl1 binding‐defective mutant (arfaptin‐1b‐F317A), consistently inhibited STxB transport. Exogenous arfaptin‐1 expression did not interfere with the localization of the Arl1‐interacting proteins golgin‐97 and golgin‐245 to the TGNand vice versa. Moreover, we found that the N‐terminal region of arfaptin‐1 was involved in the regulation of retrograde transport. Our results show that arfaptin‐1 acts as a negative regulator in Arl1‐mediated retrograde transport and suggest that different functional complexes containing Arl1 form in distinct microdomains and are responsible for different functions.

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