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Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development
Microtubule dynamics is regulated by plus end–tracking proteins (+TIPs), which localize to the plus ends of microtubules (MTs). We previously showed that TACC1 and TACC3, members of the transforming acidic coiled-coil protein family, can act as +TIPs to regulate MT dynamics in Xenopus laevis. Here w...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063610/ https://www.ncbi.nlm.nih.gov/pubmed/27559128 http://dx.doi.org/10.1091/mbc.E16-03-0198 |
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author | Rutherford, Erin L. Carandang, Leslie Ebbert, Patrick T. Mills, Alexandra N. Bowers, Jackson T. Lowery, Laura Anne |
author_facet | Rutherford, Erin L. Carandang, Leslie Ebbert, Patrick T. Mills, Alexandra N. Bowers, Jackson T. Lowery, Laura Anne |
author_sort | Rutherford, Erin L. |
collection | PubMed |
description | Microtubule dynamics is regulated by plus end–tracking proteins (+TIPs), which localize to the plus ends of microtubules (MTs). We previously showed that TACC1 and TACC3, members of the transforming acidic coiled-coil protein family, can act as +TIPs to regulate MT dynamics in Xenopus laevis. Here we characterize TACC2 as a +TIP that localizes to MT plus ends in front of EB1 and overlapping with TACC1 and TACC3 in multiple embryonic cell types. We also show that TACC2 can promote MT polymerization in mesenchymal cells but not neuronal growth cones, thus displaying cell-type specificity. Structure–function analysis demonstrates that the C-terminal region of TACC2 is both necessary and sufficient to localize to MT plus ends and promote increased rates of MT polymerization, whereas the N-terminal region cannot bind to MT plus ends but can act in a dominant-negative capacity to reduce polymerization rates. Finally, we analyze mRNA expression patterns in Xenopus embryos for each TACC protein and observe neural enrichment of TACC3 expression compared with TACC1 and TACC2, which are also expressed in mesodermal tissues, including somites. Overall these data provide a novel assessment of all three TACC proteins as a family of +TIPs by highlighting the unique attributes of each, as well as their collective characteristics. |
format | Online Article Text |
id | pubmed-5063610 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-50636102016-12-30 Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development Rutherford, Erin L. Carandang, Leslie Ebbert, Patrick T. Mills, Alexandra N. Bowers, Jackson T. Lowery, Laura Anne Mol Biol Cell Brief Reports Microtubule dynamics is regulated by plus end–tracking proteins (+TIPs), which localize to the plus ends of microtubules (MTs). We previously showed that TACC1 and TACC3, members of the transforming acidic coiled-coil protein family, can act as +TIPs to regulate MT dynamics in Xenopus laevis. Here we characterize TACC2 as a +TIP that localizes to MT plus ends in front of EB1 and overlapping with TACC1 and TACC3 in multiple embryonic cell types. We also show that TACC2 can promote MT polymerization in mesenchymal cells but not neuronal growth cones, thus displaying cell-type specificity. Structure–function analysis demonstrates that the C-terminal region of TACC2 is both necessary and sufficient to localize to MT plus ends and promote increased rates of MT polymerization, whereas the N-terminal region cannot bind to MT plus ends but can act in a dominant-negative capacity to reduce polymerization rates. Finally, we analyze mRNA expression patterns in Xenopus embryos for each TACC protein and observe neural enrichment of TACC3 expression compared with TACC1 and TACC2, which are also expressed in mesodermal tissues, including somites. Overall these data provide a novel assessment of all three TACC proteins as a family of +TIPs by highlighting the unique attributes of each, as well as their collective characteristics. The American Society for Cell Biology 2016-10-15 /pmc/articles/PMC5063610/ /pubmed/27559128 http://dx.doi.org/10.1091/mbc.E16-03-0198 Text en © 2016 Rutherford, Carandang, 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 for Cell Biology. |
spellingShingle | Brief Reports Rutherford, Erin L. Carandang, Leslie Ebbert, Patrick T. Mills, Alexandra N. Bowers, Jackson T. Lowery, Laura Anne Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title | Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title_full | Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title_fullStr | Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title_full_unstemmed | Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title_short | Xenopus TACC2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
title_sort | xenopus tacc2 is a microtubule plus end–tracking protein that can promote microtubule polymerization during embryonic development |
topic | Brief Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5063610/ https://www.ncbi.nlm.nih.gov/pubmed/27559128 http://dx.doi.org/10.1091/mbc.E16-03-0198 |
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