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Calmodulin-microtubule association in cultured mammalian cells
A Triton X-100-lysed cell system has been used to identify calmodulin on the cytoskeleton of 3T3 and transformed SV3T3 cells. By indirect immunofluorescence, calmodulin was found to be associated with both the cytoplasmic microtubule complex and the centrosomes. A number of cytoplasmic microtubules...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1984
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113150/ https://www.ncbi.nlm.nih.gov/pubmed/6365929 |
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collection | PubMed |
description | A Triton X-100-lysed cell system has been used to identify calmodulin on the cytoskeleton of 3T3 and transformed SV3T3 cells. By indirect immunofluorescence, calmodulin was found to be associated with both the cytoplasmic microtubule complex and the centrosomes. A number of cytoplasmic microtubules more resistant to disassembly upon either cold (0-4 degrees C) or hypotonic treatment, as well as following dilution have been identified. Most of the stable microtubules appeared to be associated with the centrosome at one end and with the plasma membrane at the other end. These microtubules could be induced to depolymerize, however, by micromolar Ca++ concentrations. These data suggest that, by interacting directly with the microtubule, calmodulin may influence microtubule assembly and ensure the Ca++-sensitivity of both mitotic and cytoplasmic microtubules. |
format | Text |
id | pubmed-2113150 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1984 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21131502008-05-01 Calmodulin-microtubule association in cultured mammalian cells J Cell Biol Articles A Triton X-100-lysed cell system has been used to identify calmodulin on the cytoskeleton of 3T3 and transformed SV3T3 cells. By indirect immunofluorescence, calmodulin was found to be associated with both the cytoplasmic microtubule complex and the centrosomes. A number of cytoplasmic microtubules more resistant to disassembly upon either cold (0-4 degrees C) or hypotonic treatment, as well as following dilution have been identified. Most of the stable microtubules appeared to be associated with the centrosome at one end and with the plasma membrane at the other end. These microtubules could be induced to depolymerize, however, by micromolar Ca++ concentrations. These data suggest that, by interacting directly with the microtubule, calmodulin may influence microtubule assembly and ensure the Ca++-sensitivity of both mitotic and cytoplasmic microtubules. The Rockefeller University Press 1984-03-01 /pmc/articles/PMC2113150/ /pubmed/6365929 Text en 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.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Calmodulin-microtubule association in cultured mammalian cells |
title | Calmodulin-microtubule association in cultured mammalian cells |
title_full | Calmodulin-microtubule association in cultured mammalian cells |
title_fullStr | Calmodulin-microtubule association in cultured mammalian cells |
title_full_unstemmed | Calmodulin-microtubule association in cultured mammalian cells |
title_short | Calmodulin-microtubule association in cultured mammalian cells |
title_sort | calmodulin-microtubule association in cultured mammalian cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113150/ https://www.ncbi.nlm.nih.gov/pubmed/6365929 |