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Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole
The hexameric HOPS (homotypic fusion and protein sorting) complex is a conserved tethering complex at the lysosome-like vacuole, where it mediates tethering and promotes all fusion events involving this organelle. The Vps39 subunit of this complex also engages in a membrane contact site between the...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694092/ https://www.ncbi.nlm.nih.gov/pubmed/34668759 http://dx.doi.org/10.1091/mbc.E21-05-0227 |
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author | González Montoro, Ayelén Vargas Duarte, Prado Auffarth, Kathrin Walter, Stefan Fröhlich, Florian Ungermann, Christian |
author_facet | González Montoro, Ayelén Vargas Duarte, Prado Auffarth, Kathrin Walter, Stefan Fröhlich, Florian Ungermann, Christian |
author_sort | González Montoro, Ayelén |
collection | PubMed |
description | The hexameric HOPS (homotypic fusion and protein sorting) complex is a conserved tethering complex at the lysosome-like vacuole, where it mediates tethering and promotes all fusion events involving this organelle. The Vps39 subunit of this complex also engages in a membrane contact site between the vacuole and the mitochondria, called vCLAMP. Additionally, four subunits of HOPS are also part of the endosomal CORVET tethering complex. Here, we analyzed the partition of HOPS and CORVET subunits between the different complexes by tracing their localization and function. We find that Vps39 has a specific role in vCLAMP formation beyond tethering, and that vCLAMPs and HOPS compete for the same pool of Vps39. In agreement, we find that the CORVET subunit Vps3 can take the position of Vps39 in HOPS. This endogenous pool of a Vps3-hybrid complex is affected by Vps3 or Vps39 levels, suggesting that HOPS and CORVET assembly is dynamic. Our data shed light on how individual subunits of tethering complexes such as Vps39 can participate in other functions, while maintaining the remaining subcomplex available for its function in tethering and fusion. |
format | Online Article Text |
id | pubmed-8694092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-86940922022-02-16 Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole González Montoro, Ayelén Vargas Duarte, Prado Auffarth, Kathrin Walter, Stefan Fröhlich, Florian Ungermann, Christian Mol Biol Cell Brief Reports The hexameric HOPS (homotypic fusion and protein sorting) complex is a conserved tethering complex at the lysosome-like vacuole, where it mediates tethering and promotes all fusion events involving this organelle. The Vps39 subunit of this complex also engages in a membrane contact site between the vacuole and the mitochondria, called vCLAMP. Additionally, four subunits of HOPS are also part of the endosomal CORVET tethering complex. Here, we analyzed the partition of HOPS and CORVET subunits between the different complexes by tracing their localization and function. We find that Vps39 has a specific role in vCLAMP formation beyond tethering, and that vCLAMPs and HOPS compete for the same pool of Vps39. In agreement, we find that the CORVET subunit Vps3 can take the position of Vps39 in HOPS. This endogenous pool of a Vps3-hybrid complex is affected by Vps3 or Vps39 levels, suggesting that HOPS and CORVET assembly is dynamic. Our data shed light on how individual subunits of tethering complexes such as Vps39 can participate in other functions, while maintaining the remaining subcomplex available for its function in tethering and fusion. The American Society for Cell Biology 2021-12-01 /pmc/articles/PMC8694092/ /pubmed/34668759 http://dx.doi.org/10.1091/mbc.E21-05-0227 Text en © 2021 González Montoro et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International Creative Commons License. |
spellingShingle | Brief Reports González Montoro, Ayelén Vargas Duarte, Prado Auffarth, Kathrin Walter, Stefan Fröhlich, Florian Ungermann, Christian Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title | Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title_full | Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title_fullStr | Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title_full_unstemmed | Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title_short | Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
title_sort | subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole |
topic | Brief Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8694092/ https://www.ncbi.nlm.nih.gov/pubmed/34668759 http://dx.doi.org/10.1091/mbc.E21-05-0227 |
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