Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos
Upon entry into mitosis, many microtubules are nucleated that coordinately integrate into a stable, yet dynamic, mitotic spindle apparatus. In a recent publication, we examined microtubule-generating pathways within a single model system, the Drosophila syncytial embryo. We found that, following dep...
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| Format: | Online |
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Landes Bioscience
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091100/ |
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pubmed-4091100 |
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pubmed-40911002014-07-22 Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos Hayward, Daniel Wakefield, James G Article Addendum Upon entry into mitosis, many microtubules are nucleated that coordinately integrate into a stable, yet dynamic, mitotic spindle apparatus. In a recent publication, we examined microtubule-generating pathways within a single model system, the Drosophila syncytial embryo. We found that, following depolymerisation of metaphase spindle microtubules by cold treatment, spindles regenerate predominantly from microtubules nucleated within the vicinity of chromatin. We also showed this chromatin-mediated microtubule nucleation is mediated by the Drosophila homolog of a vertebrate spindle assembly factor (SAF), HURP and is dependent on the conserved microtubule amplifying protein complex, Augmin. Here, we expand our investigation into Drosophila SAFs, providing evidence that, in vitro, both D-HURP and D-TPX2 are able to bind to and stabilize microtubules. We show that GFP-D-HURP purified from embryos interacts with Importin-β and Augmin and, consistent with this, demonstrate that the underlying basis of chromatin-mediated microtubule nucleation in Drosophila syncytial embryos is dependent on Ran-GTP. Landes Bioscience 2014-04-02 /pmc/articles/PMC4091100/ /pubmed/25053984 http://dx.doi.org/10.4161/cib.28512 Text en Copyright © 2014 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Hayward, Daniel Wakefield, James G |
| spellingShingle |
Hayward, Daniel Wakefield, James G Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| author_facet |
Hayward, Daniel Wakefield, James G |
| author_sort |
Hayward, Daniel |
| title |
Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| title_short |
Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| title_full |
Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| title_fullStr |
Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| title_full_unstemmed |
Chromatin-mediated microtubule nucleation in Drosophila syncytial embryos |
| title_sort |
chromatin-mediated microtubule nucleation in drosophila syncytial embryos |
| description |
Upon entry into mitosis, many microtubules are nucleated that coordinately integrate into a stable, yet dynamic, mitotic spindle apparatus. In a recent publication, we examined microtubule-generating pathways within a single model system, the Drosophila syncytial embryo. We found that, following depolymerisation of metaphase spindle microtubules by cold treatment, spindles regenerate predominantly from microtubules nucleated within the vicinity of chromatin. We also showed this chromatin-mediated microtubule nucleation is mediated by the Drosophila homolog of a vertebrate spindle assembly factor (SAF), HURP and is dependent on the conserved microtubule amplifying protein complex, Augmin. Here, we expand our investigation into Drosophila SAFs, providing evidence that, in vitro, both D-HURP and D-TPX2 are able to bind to and stabilize microtubules. We show that GFP-D-HURP purified from embryos interacts with Importin-β and Augmin and, consistent with this, demonstrate that the underlying basis of chromatin-mediated microtubule nucleation in Drosophila syncytial embryos is dependent on Ran-GTP. |
| publisher |
Landes Bioscience |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4091100/ |
| _version_ |
1613111222322855936 |