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CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology
Mitochondria are dynamic organelles that frequently move, divide, and fuse with one another to maintain their architecture and functions. However, the signaling mechanisms involved in these processes are still not well characterized. In this study, we analyze mitochondrial dynamics and morphology in...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2500141/ https://www.ncbi.nlm.nih.gov/pubmed/18695047 http://dx.doi.org/10.1083/jcb.200802164 |
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author | Han, Xiao-Jian Lu, Yun-Fei Li, Shun-Ai Kaitsuka, Taku Sato, Yasufumi Tomizawa, Kazuhito Nairn, Angus C. Takei, Kohji Matsui, Hideki Matsushita, Masayuki |
author_facet | Han, Xiao-Jian Lu, Yun-Fei Li, Shun-Ai Kaitsuka, Taku Sato, Yasufumi Tomizawa, Kazuhito Nairn, Angus C. Takei, Kohji Matsui, Hideki Matsushita, Masayuki |
author_sort | Han, Xiao-Jian |
collection | PubMed |
description | Mitochondria are dynamic organelles that frequently move, divide, and fuse with one another to maintain their architecture and functions. However, the signaling mechanisms involved in these processes are still not well characterized. In this study, we analyze mitochondrial dynamics and morphology in neurons. Using time-lapse imaging, we find that Ca(2+) influx through voltage-dependent Ca(2+) channels (VDCCs) causes a rapid halt in mitochondrial movement and induces mitochondrial fission. VDCC-associated Ca(2+) signaling stimulates phosphorylation of dynamin-related protein 1 (Drp1) at serine 600 via activation of Ca(2+)/calmodulin-dependent protein kinase Iα (CaMKIα). In neurons and HeLa cells, phosphorylation of Drp1 at serine 600 is associated with an increase in Drp1 translocation to mitochondria, whereas in vitro, phosphorylation of Drp1 results in an increase in its affinity for Fis1. CaMKIα is a widely expressed protein kinase, suggesting that Ca(2+) is likely to be functionally important in the control of mitochondrial dynamics through regulation of Drp1 phosphorylation in neurons and other cell types. |
format | Text |
id | pubmed-2500141 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-25001412009-02-11 CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology Han, Xiao-Jian Lu, Yun-Fei Li, Shun-Ai Kaitsuka, Taku Sato, Yasufumi Tomizawa, Kazuhito Nairn, Angus C. Takei, Kohji Matsui, Hideki Matsushita, Masayuki J Cell Biol Research Articles Mitochondria are dynamic organelles that frequently move, divide, and fuse with one another to maintain their architecture and functions. However, the signaling mechanisms involved in these processes are still not well characterized. In this study, we analyze mitochondrial dynamics and morphology in neurons. Using time-lapse imaging, we find that Ca(2+) influx through voltage-dependent Ca(2+) channels (VDCCs) causes a rapid halt in mitochondrial movement and induces mitochondrial fission. VDCC-associated Ca(2+) signaling stimulates phosphorylation of dynamin-related protein 1 (Drp1) at serine 600 via activation of Ca(2+)/calmodulin-dependent protein kinase Iα (CaMKIα). In neurons and HeLa cells, phosphorylation of Drp1 at serine 600 is associated with an increase in Drp1 translocation to mitochondria, whereas in vitro, phosphorylation of Drp1 results in an increase in its affinity for Fis1. CaMKIα is a widely expressed protein kinase, suggesting that Ca(2+) is likely to be functionally important in the control of mitochondrial dynamics through regulation of Drp1 phosphorylation in neurons and other cell types. The Rockefeller University Press 2008-08-11 /pmc/articles/PMC2500141/ /pubmed/18695047 http://dx.doi.org/10.1083/jcb.200802164 Text en © 2008 Han et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Han, Xiao-Jian Lu, Yun-Fei Li, Shun-Ai Kaitsuka, Taku Sato, Yasufumi Tomizawa, Kazuhito Nairn, Angus C. Takei, Kohji Matsui, Hideki Matsushita, Masayuki CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title | CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title_full | CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title_fullStr | CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title_full_unstemmed | CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title_short | CaM kinase Iα–induced phosphorylation of Drp1 regulates mitochondrial morphology |
title_sort | cam kinase iα–induced phosphorylation of drp1 regulates mitochondrial morphology |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2500141/ https://www.ncbi.nlm.nih.gov/pubmed/18695047 http://dx.doi.org/10.1083/jcb.200802164 |
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