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The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p
The exomer complex is a putative vesicle coat required for the direct transport of a subset of cargoes from the trans-Golgi network (TGN) to the plasma membrane. Exomer comprises Chs5p and the ChAPs family of proteins (Chs6p, Bud7p, Bch1p, and Bch2p), which are believed to act as cargo receptors. In...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496614/ https://www.ncbi.nlm.nih.gov/pubmed/23015758 http://dx.doi.org/10.1091/mbc.E11-12-1015 |
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author | Rockenbauch, Uli Ritz, Alicja M. Sacristan, Carlos Roncero, Cesar Spang, Anne |
author_facet | Rockenbauch, Uli Ritz, Alicja M. Sacristan, Carlos Roncero, Cesar Spang, Anne |
author_sort | Rockenbauch, Uli |
collection | PubMed |
description | The exomer complex is a putative vesicle coat required for the direct transport of a subset of cargoes from the trans-Golgi network (TGN) to the plasma membrane. Exomer comprises Chs5p and the ChAPs family of proteins (Chs6p, Bud7p, Bch1p, and Bch2p), which are believed to act as cargo receptors. In particular, Chs6p is required for the transport of the chitin synthase Chs3p to the bud neck. However, how the ChAPs associate with Chs5p and recognize cargo is not well understood. Using domain-switch chimeras of Chs6p and Bch2p, we show that four tetratricopeptide repeats (TPRs) are involved in interaction with Chs5p. Because these roles are conserved among the ChAPs, the TPRs are interchangeable among different ChAP proteins. In contrast, the N-terminal and the central parts of the ChAPs contribute to cargo specificity. Although the entire N-terminal domain of Chs6p is required for Chs3p export at all cell cycle stages, the central part seems to predominantly favor Chs3p export in small-budded cells. The cargo Chs3p probably also uses a complex motif for the interaction with Chs6, as the C-terminus of Chs3p interacts with Chs6p and is necessary, but not sufficient, for TGN export. |
format | Online Article Text |
id | pubmed-3496614 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34966142013-01-30 The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p Rockenbauch, Uli Ritz, Alicja M. Sacristan, Carlos Roncero, Cesar Spang, Anne Mol Biol Cell Articles The exomer complex is a putative vesicle coat required for the direct transport of a subset of cargoes from the trans-Golgi network (TGN) to the plasma membrane. Exomer comprises Chs5p and the ChAPs family of proteins (Chs6p, Bud7p, Bch1p, and Bch2p), which are believed to act as cargo receptors. In particular, Chs6p is required for the transport of the chitin synthase Chs3p to the bud neck. However, how the ChAPs associate with Chs5p and recognize cargo is not well understood. Using domain-switch chimeras of Chs6p and Bch2p, we show that four tetratricopeptide repeats (TPRs) are involved in interaction with Chs5p. Because these roles are conserved among the ChAPs, the TPRs are interchangeable among different ChAP proteins. In contrast, the N-terminal and the central parts of the ChAPs contribute to cargo specificity. Although the entire N-terminal domain of Chs6p is required for Chs3p export at all cell cycle stages, the central part seems to predominantly favor Chs3p export in small-budded cells. The cargo Chs3p probably also uses a complex motif for the interaction with Chs6, as the C-terminus of Chs3p interacts with Chs6p and is necessary, but not sufficient, for TGN export. The American Society for Cell Biology 2012-11-15 /pmc/articles/PMC3496614/ /pubmed/23015758 http://dx.doi.org/10.1091/mbc.E11-12-1015 Text en © 2012 Rockenbauch et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Rockenbauch, Uli Ritz, Alicja M. Sacristan, Carlos Roncero, Cesar Spang, Anne The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title | The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title_full | The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title_fullStr | The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title_full_unstemmed | The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title_short | The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p |
title_sort | complex interactions of chs5p, the chaps, and the cargo chs3p |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496614/ https://www.ncbi.nlm.nih.gov/pubmed/23015758 http://dx.doi.org/10.1091/mbc.E11-12-1015 |
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