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Assembly of the AAA ATPase Vps4 on ESCRT-III
Vps4 is a key enzyme that functions in endosomal protein trafficking, cytokinesis, and retroviral budding. Vps4 activity is regulated by its recruitment from the cytoplasm to ESCRT-III, where the protein oligomerizes into an active ATPase. The recruitment and oligomerization steps are mediated by a...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836958/ https://www.ncbi.nlm.nih.gov/pubmed/20110351 http://dx.doi.org/10.1091/mbc.E09-07-0572 |
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author | Shestakova, Anna Hanono, Abraham Drosner, Stacey Curtiss, Matt Davies, Brian A. Katzmann, David J. Babst, Markus |
author_facet | Shestakova, Anna Hanono, Abraham Drosner, Stacey Curtiss, Matt Davies, Brian A. Katzmann, David J. Babst, Markus |
author_sort | Shestakova, Anna |
collection | PubMed |
description | Vps4 is a key enzyme that functions in endosomal protein trafficking, cytokinesis, and retroviral budding. Vps4 activity is regulated by its recruitment from the cytoplasm to ESCRT-III, where the protein oligomerizes into an active ATPase. The recruitment and oligomerization steps are mediated by a complex network of at least 12 distinct interactions between Vps4, ESCRT-III, Ist1, Vta1, and Did2. The order of events leading to active, ESCRT-III–associated Vps4 is poorly understood. In this study we present a systematic in vivo analysis of the Vps4 interaction network. The data demonstrated a high degree of redundancy in the network. Although no single interaction was found to be essential for the localization or activity of Vps4, certain interactions proved more important than others. The most significant among these were the binding of Vps4 to Vta1 and to the ESCRT-III subunits Vps2 and Snf7. In our model we propose the formation of a recruitment complex in the cytoplasm that is composed of Did2-Ist1-Vps4, which upon binding to ESCRT-III recruits Vta1. Vta1 in turn is predicted to cause a rearrangement of the Vps4 interactions that initiates the assembly of the active Vps4 oligomer. |
format | Text |
id | pubmed-2836958 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-28369582010-05-30 Assembly of the AAA ATPase Vps4 on ESCRT-III Shestakova, Anna Hanono, Abraham Drosner, Stacey Curtiss, Matt Davies, Brian A. Katzmann, David J. Babst, Markus Mol Biol Cell Articles Vps4 is a key enzyme that functions in endosomal protein trafficking, cytokinesis, and retroviral budding. Vps4 activity is regulated by its recruitment from the cytoplasm to ESCRT-III, where the protein oligomerizes into an active ATPase. The recruitment and oligomerization steps are mediated by a complex network of at least 12 distinct interactions between Vps4, ESCRT-III, Ist1, Vta1, and Did2. The order of events leading to active, ESCRT-III–associated Vps4 is poorly understood. In this study we present a systematic in vivo analysis of the Vps4 interaction network. The data demonstrated a high degree of redundancy in the network. Although no single interaction was found to be essential for the localization or activity of Vps4, certain interactions proved more important than others. The most significant among these were the binding of Vps4 to Vta1 and to the ESCRT-III subunits Vps2 and Snf7. In our model we propose the formation of a recruitment complex in the cytoplasm that is composed of Did2-Ist1-Vps4, which upon binding to ESCRT-III recruits Vta1. Vta1 in turn is predicted to cause a rearrangement of the Vps4 interactions that initiates the assembly of the active Vps4 oligomer. The American Society for Cell Biology 2010-03-15 /pmc/articles/PMC2836958/ /pubmed/20110351 http://dx.doi.org/10.1091/mbc.E09-07-0572 Text en © 2010 by The American Society for Cell Biology |
spellingShingle | Articles Shestakova, Anna Hanono, Abraham Drosner, Stacey Curtiss, Matt Davies, Brian A. Katzmann, David J. Babst, Markus Assembly of the AAA ATPase Vps4 on ESCRT-III |
title | Assembly of the AAA ATPase Vps4 on ESCRT-III |
title_full | Assembly of the AAA ATPase Vps4 on ESCRT-III |
title_fullStr | Assembly of the AAA ATPase Vps4 on ESCRT-III |
title_full_unstemmed | Assembly of the AAA ATPase Vps4 on ESCRT-III |
title_short | Assembly of the AAA ATPase Vps4 on ESCRT-III |
title_sort | assembly of the aaa atpase vps4 on escrt-iii |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836958/ https://www.ncbi.nlm.nih.gov/pubmed/20110351 http://dx.doi.org/10.1091/mbc.E09-07-0572 |
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