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Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles
The main function of background two-pore potassium (K(2P)) channels KCNK3/9/15 is to stabilize the cell membrane potential. We previously observed that membrane potential depolarization enhances the release of HIV-1 viruses. Because membrane polarization affects the biomembrane directly, here we exa...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Humana Press Inc
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090673/ https://www.ncbi.nlm.nih.gov/pubmed/21761257 http://dx.doi.org/10.1007/s12013-011-9241-1 |
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author | Huang, Daniel Tsung-Ning Chi, Naiwen Chen, Shiou-Ching Lee, Ting-Ying Hsu, Kate |
author_facet | Huang, Daniel Tsung-Ning Chi, Naiwen Chen, Shiou-Ching Lee, Ting-Ying Hsu, Kate |
author_sort | Huang, Daniel Tsung-Ning |
collection | PubMed |
description | The main function of background two-pore potassium (K(2P)) channels KCNK3/9/15 is to stabilize the cell membrane potential. We previously observed that membrane potential depolarization enhances the release of HIV-1 viruses. Because membrane polarization affects the biomembrane directly, here we examined the effects of KCNK3/9/15 on the budding of nonviral vesicles. We found that depolarization by knocking down endogenous KCNK3/9/15 promoted secretion of cell-derived vesicles. We further used Vpu (an antagonist of KCNK3) as a model for the in vivo study of depolarization-stimulated secretion. Vpu is a HIV-1-encoded, ion channel-like protein (viroporin) capable of enhancing virus release and depolarizing the cell membrane potential. We found that Vpu could also promote nonviral vesicle release, perhaps through a similar mechanism that Vpu utilizes to promote viral particle release. Notably, T cells expressing Vpu alone became pathologically low in intracellular K(+) and insensitive to extracellular K(+) or membrane potential stimulation. In contrast, heterologous expression of KCNK3 in T cells stabilized the cell potentials by maintaining intracellular K(+). We thus concluded that KCNK3/9/15 expression limits membrane depolarization and depolarization-induced secretion at least in part by maintaining intracellular K(+). |
format | Online Article Text |
id | pubmed-7090673 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Humana Press Inc |
record_format | MEDLINE/PubMed |
spelling | pubmed-70906732020-03-24 Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles Huang, Daniel Tsung-Ning Chi, Naiwen Chen, Shiou-Ching Lee, Ting-Ying Hsu, Kate Cell Biochem Biophys Original Paper The main function of background two-pore potassium (K(2P)) channels KCNK3/9/15 is to stabilize the cell membrane potential. We previously observed that membrane potential depolarization enhances the release of HIV-1 viruses. Because membrane polarization affects the biomembrane directly, here we examined the effects of KCNK3/9/15 on the budding of nonviral vesicles. We found that depolarization by knocking down endogenous KCNK3/9/15 promoted secretion of cell-derived vesicles. We further used Vpu (an antagonist of KCNK3) as a model for the in vivo study of depolarization-stimulated secretion. Vpu is a HIV-1-encoded, ion channel-like protein (viroporin) capable of enhancing virus release and depolarizing the cell membrane potential. We found that Vpu could also promote nonviral vesicle release, perhaps through a similar mechanism that Vpu utilizes to promote viral particle release. Notably, T cells expressing Vpu alone became pathologically low in intracellular K(+) and insensitive to extracellular K(+) or membrane potential stimulation. In contrast, heterologous expression of KCNK3 in T cells stabilized the cell potentials by maintaining intracellular K(+). We thus concluded that KCNK3/9/15 expression limits membrane depolarization and depolarization-induced secretion at least in part by maintaining intracellular K(+). Humana Press Inc 2011-07-15 2011 /pmc/articles/PMC7090673/ /pubmed/21761257 http://dx.doi.org/10.1007/s12013-011-9241-1 Text en © Springer Science+Business Media, LLC 2011 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Original Paper Huang, Daniel Tsung-Ning Chi, Naiwen Chen, Shiou-Ching Lee, Ting-Ying Hsu, Kate Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title | Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title_full | Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title_fullStr | Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title_full_unstemmed | Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title_short | Background K(2P) Channels KCNK3/9/15 Limit the Budding of Cell Membrane-derived Vesicles |
title_sort | background k(2p) channels kcnk3/9/15 limit the budding of cell membrane-derived vesicles |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7090673/ https://www.ncbi.nlm.nih.gov/pubmed/21761257 http://dx.doi.org/10.1007/s12013-011-9241-1 |
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