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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...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2010
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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. |
format | Text |
id | pubmed-2947474 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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