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Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex

The Golgi-associated retrograde protein (GARP) complex mediates tethering and fusion of endosome-derived transport carriers to the trans-Golgi network (TGN). In the yeast Saccharomyces cerevisiae, GARP comprises four subunits named Vps51p, Vps52p, Vps53p, and Vps54p. Orthologues of the GARP subunits...

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Autores principales: Pérez-Victoria, F. Javier, Schindler, Christina, Magadán, Javier G., Mardones, Gonzalo A., Delevoye, Cédric, Romao, Maryse, Raposo, Graça, Bonifacino, Juan S.
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2947474/
https://www.ncbi.nlm.nih.gov/pubmed/20685960
http://dx.doi.org/10.1091/mbc.E10-05-0392
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author Pérez-Victoria, F. Javier
Schindler, Christina
Magadán, Javier G.
Mardones, Gonzalo A.
Delevoye, Cédric
Romao, Maryse
Raposo, Graça
Bonifacino, Juan S.
author_facet Pérez-Victoria, F. Javier
Schindler, Christina
Magadán, Javier G.
Mardones, Gonzalo A.
Delevoye, Cédric
Romao, Maryse
Raposo, Graça
Bonifacino, Juan S.
author_sort Pérez-Victoria, F. Javier
collection PubMed
description The Golgi-associated retrograde protein (GARP) complex mediates tethering and fusion of endosome-derived transport carriers to the trans-Golgi network (TGN). In the yeast Saccharomyces cerevisiae, GARP comprises four subunits named Vps51p, Vps52p, Vps53p, and Vps54p. Orthologues of the GARP subunits, except for Vps51p, have been identified in all other eukaryotes. A yeast two-hybrid screen of a human cDNA library yielded a phylogenetically conserved protein, Ang2/Fat-free, which interacts with human Vps52, Vps53 and Vps54. Human Ang2 is larger than yeast Vps51p, but exhibits significant homology in an N-terminal coiled-coil region that mediates assembly with other GARP subunits. Biochemical analyses show that human Ang2, Vps52, Vps53 and Vps54 form an obligatory 1:1:1:1 complex that strongly interacts with the regulatory Habc domain of the TGN SNARE, Syntaxin 6. Depletion of Ang2 or the GARP subunits similarly impairs protein retrieval to the TGN, lysosomal enzyme sorting, endosomal cholesterol traffic¤ and autophagy. These findings indicate that Ang2 is the missing component of the GARP complex in most eukaryotes.
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spelling pubmed-29474742010-12-16 Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex Pérez-Victoria, F. Javier Schindler, Christina Magadán, Javier G. Mardones, Gonzalo A. Delevoye, Cédric Romao, Maryse Raposo, Graça Bonifacino, Juan S. Mol Biol Cell Articles The Golgi-associated retrograde protein (GARP) complex mediates tethering and fusion of endosome-derived transport carriers to the trans-Golgi network (TGN). In the yeast Saccharomyces cerevisiae, GARP comprises four subunits named Vps51p, Vps52p, Vps53p, and Vps54p. Orthologues of the GARP subunits, except for Vps51p, have been identified in all other eukaryotes. A yeast two-hybrid screen of a human cDNA library yielded a phylogenetically conserved protein, Ang2/Fat-free, which interacts with human Vps52, Vps53 and Vps54. Human Ang2 is larger than yeast Vps51p, but exhibits significant homology in an N-terminal coiled-coil region that mediates assembly with other GARP subunits. Biochemical analyses show that human Ang2, Vps52, Vps53 and Vps54 form an obligatory 1:1:1:1 complex that strongly interacts with the regulatory Habc domain of the TGN SNARE, Syntaxin 6. Depletion of Ang2 or the GARP subunits similarly impairs protein retrieval to the TGN, lysosomal enzyme sorting, endosomal cholesterol traffic¤ and autophagy. These findings indicate that Ang2 is the missing component of the GARP complex in most eukaryotes. The American Society for Cell Biology 2010-10-01 /pmc/articles/PMC2947474/ /pubmed/20685960 http://dx.doi.org/10.1091/mbc.E10-05-0392 Text en © 2010 by The American Society for Cell Biology
spellingShingle Articles
Pérez-Victoria, F. Javier
Schindler, Christina
Magadán, Javier G.
Mardones, Gonzalo A.
Delevoye, Cédric
Romao, Maryse
Raposo, Graça
Bonifacino, Juan S.
Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title_full Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title_fullStr Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title_full_unstemmed Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title_short Ang2/Fat-Free Is a Conserved Subunit of the Golgi-associated Retrograde Protein Complex
title_sort ang2/fat-free is a conserved subunit of the golgi-associated retrograde protein complex
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2947474/
https://www.ncbi.nlm.nih.gov/pubmed/20685960
http://dx.doi.org/10.1091/mbc.E10-05-0392
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