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HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage

More than a decade has elapsed since the link between the endosomal sorting complex required for transport (ESCRT) machinery and HIV-1 protein trafficking and budding was first identified. L domains in HIV-1 Gag mediate recruitment of ESCRT which function in bud abscission releasing the viral partic...

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Detalles Bibliográficos
Autores principales: Ehrlich, Lorna S., Carter, Carol A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384956/
https://www.ncbi.nlm.nih.gov/pubmed/22761998
http://dx.doi.org/10.1155/2012/851670
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author Ehrlich, Lorna S.
Carter, Carol A.
author_facet Ehrlich, Lorna S.
Carter, Carol A.
author_sort Ehrlich, Lorna S.
collection PubMed
description More than a decade has elapsed since the link between the endosomal sorting complex required for transport (ESCRT) machinery and HIV-1 protein trafficking and budding was first identified. L domains in HIV-1 Gag mediate recruitment of ESCRT which function in bud abscission releasing the viral particle from the host cell. Beyond virus budding, the ESCRT machinery is also involved in the endocytic pathway, cytokinesis, and autophagy. In the past few years, the number of non-ESCRT host proteins shown to be required in the assembly process has also grown. In this paper, we highlight the role of recently identified cellular factors that link ESCRT machinery to calcium signaling machinery and we suggest that this liaison contributes to setting the stage for productive ESCRT recruitment and mediation of abscission. Parallel paradigms for non-ESCRT roles in virus budding and cytokinesis will be discussed.
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spelling pubmed-33849562012-07-03 HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage Ehrlich, Lorna S. Carter, Carol A. Mol Biol Int Review Article More than a decade has elapsed since the link between the endosomal sorting complex required for transport (ESCRT) machinery and HIV-1 protein trafficking and budding was first identified. L domains in HIV-1 Gag mediate recruitment of ESCRT which function in bud abscission releasing the viral particle from the host cell. Beyond virus budding, the ESCRT machinery is also involved in the endocytic pathway, cytokinesis, and autophagy. In the past few years, the number of non-ESCRT host proteins shown to be required in the assembly process has also grown. In this paper, we highlight the role of recently identified cellular factors that link ESCRT machinery to calcium signaling machinery and we suggest that this liaison contributes to setting the stage for productive ESCRT recruitment and mediation of abscission. Parallel paradigms for non-ESCRT roles in virus budding and cytokinesis will be discussed. Hindawi Publishing Corporation 2012 2012-06-12 /pmc/articles/PMC3384956/ /pubmed/22761998 http://dx.doi.org/10.1155/2012/851670 Text en Copyright © 2012 L. S. Ehrlich and C. A. Carter. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Ehrlich, Lorna S.
Carter, Carol A.
HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title_full HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title_fullStr HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title_full_unstemmed HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title_short HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage
title_sort hiv assembly and budding: ca(2+) signaling and non-escrt proteins set the stage
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384956/
https://www.ncbi.nlm.nih.gov/pubmed/22761998
http://dx.doi.org/10.1155/2012/851670
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