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• W2044897203 startingPage "e0118743" @default.
• W2044897203 abstract "The small 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 novel function 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 TGN and 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." @default.
• W2044897203 created "2016-06-24" @default.
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• W2044897203 date "2015-03-19" @default.
• W2044897203 modified "2023-10-18" @default.
• W2044897203 title "Arfaptin-1 Negatively Regulates Arl1-Mediated Retrograde Transport" @default.
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• W2044897203 doi "https://doi.org/10.1371/journal.pone.0118743" @default.
• W2044897203 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4366199" @default.
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• W2044897203 hasPublicationYear "2015" @default.
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