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Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane
Voltage-gated K(+) (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and...
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/PMC3408418/ https://www.ncbi.nlm.nih.gov/pubmed/22648171 http://dx.doi.org/10.1091/mbc.E12-01-0047 |
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author | Deutsch, Emily Weigel, Aubrey V. Akin, Elizabeth J. Fox, Phil Hansen, Gentry Haberkorn, Christopher J. Loftus, Rob Krapf, Diego Tamkun, Michael M. |
author_facet | Deutsch, Emily Weigel, Aubrey V. Akin, Elizabeth J. Fox, Phil Hansen, Gentry Haberkorn, Christopher J. Loftus, Rob Krapf, Diego Tamkun, Michael M. |
author_sort | Deutsch, Emily |
collection | PubMed |
description | Voltage-gated K(+) (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and transfected human embryonic kidney (HEK) cells, where it is nonconducting. Because Kv2.1 is postulated to be involved in soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion, we examined the hypothesis that these surface clusters are specialized platforms involved in membrane protein trafficking. Total internal reflection–based fluorescence recovery after photobleaching studies and quantum dot imaging of single Kv2.1 channels revealed that Kv2.1-containing vesicles deliver cargo at the Kv2.1 surface clusters in both transfected HEK cells and hippocampal neurons. More than 85% of cytoplasmic and recycling Kv2.1 channels was delivered to the cell surface at the cluster perimeter in both cell types. At least 85% of recycling Kv1.4, which, unlike Kv2.1, has a homogeneous surface distribution, is also delivered here. Actin depolymerization resulted in Kv2.1 exocytosis at cluster-free surface membrane. These results indicate that one nonconducting function of Kv2.1 is to form microdomains involved in membrane protein trafficking. This study is the first to identify stable cell surface platforms involved in ion channel trafficking. |
format | Online Article Text |
id | pubmed-3408418 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34084182012-10-16 Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane Deutsch, Emily Weigel, Aubrey V. Akin, Elizabeth J. Fox, Phil Hansen, Gentry Haberkorn, Christopher J. Loftus, Rob Krapf, Diego Tamkun, Michael M. Mol Biol Cell Articles Voltage-gated K(+) (Kv) channels regulate membrane potential in many cell types. Although the channel surface density and location must be well controlled, little is known about Kv channel delivery and retrieval on the cell surface. The Kv2.1 channel localizes to micron-sized clusters in neurons and transfected human embryonic kidney (HEK) cells, where it is nonconducting. Because Kv2.1 is postulated to be involved in soluble N-ethylmaleimide–sensitive factor attachment protein receptor–mediated membrane fusion, we examined the hypothesis that these surface clusters are specialized platforms involved in membrane protein trafficking. Total internal reflection–based fluorescence recovery after photobleaching studies and quantum dot imaging of single Kv2.1 channels revealed that Kv2.1-containing vesicles deliver cargo at the Kv2.1 surface clusters in both transfected HEK cells and hippocampal neurons. More than 85% of cytoplasmic and recycling Kv2.1 channels was delivered to the cell surface at the cluster perimeter in both cell types. At least 85% of recycling Kv1.4, which, unlike Kv2.1, has a homogeneous surface distribution, is also delivered here. Actin depolymerization resulted in Kv2.1 exocytosis at cluster-free surface membrane. These results indicate that one nonconducting function of Kv2.1 is to form microdomains involved in membrane protein trafficking. This study is the first to identify stable cell surface platforms involved in ion channel trafficking. The American Society for Cell Biology 2012-08-01 /pmc/articles/PMC3408418/ /pubmed/22648171 http://dx.doi.org/10.1091/mbc.E12-01-0047 Text en © 2012 Deutsch 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 Deutsch, Emily Weigel, Aubrey V. Akin, Elizabeth J. Fox, Phil Hansen, Gentry Haberkorn, Christopher J. Loftus, Rob Krapf, Diego Tamkun, Michael M. Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title | Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title_full | Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title_fullStr | Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title_full_unstemmed | Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title_short | Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
title_sort | kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3408418/ https://www.ncbi.nlm.nih.gov/pubmed/22648171 http://dx.doi.org/10.1091/mbc.E12-01-0047 |
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