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Proc Natl Acad Sci U S A. 2002 May 14;99(10):6755-60. Epub 2002 May 7.

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

Author information

1
Department of Cell Biology and the Institute for Childhood and Neglected Diseases, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

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.

PMID:
11997454
PMCID:
PMC124475
DOI:
10.1073/pnas.092150699
[Indexed for MEDLINE]
Free PMC Article

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