NDLI: The δ subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface

Content Provider	PubMed Central
Author	Nishimura, Noriyuki Helen, Plutner Hahn, Klaus Balch, William E.
Copyright Year	2002
Abstract	Vesicular stomatitis virus glycoprotein (VSV-G) is a transmembrane protein that functions as the surface coat of enveloped viral particles. We report the surprising result that VSV-G uses the tyrosine-based di-acidic motif (-YTDIE-) found in its cytoplasmic tail to recruit adaptor protein complex 3 for export from the trans-Golgi network. The same sorting code is used to recruit coat complex II to direct efficient transport from the endoplasmic reticulum to the Golgi apparatus. These results demonstrate that a single sorting sequence can interact with sequential coat machineries to direct transport through the secretory pathway. We propose that use of this compact sorting domain reflects a need for both efficient endoplasmic reticulum export and concentration of VSV-G into specialized post-trans-Golgi network secretory-lysosome type transport containers to facilitate formation of viral coats at the cell surface.
Related Links	http://dx.doi.org/10.1073/pnas.092150699
Ending Page	6760
Page Count	6
Starting Page	6755
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	99
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2002-05-14
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface.

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