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Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
Little is known about how microtubules are regulated in different cell types during development. EB1 plays a central role in the regulation of microtubule plus ends. It directly binds to microtubule plus ends and recruits proteins which regulate microtubule dynamics and behaviour. We report the iden...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159139/ https://www.ncbi.nlm.nih.gov/pubmed/25203404 http://dx.doi.org/10.1371/journal.pone.0106112 |
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author | Clohisey, Sara M. R. Dzhindzhev, Nikola S. Ohkura, Hiroyuki |
author_facet | Clohisey, Sara M. R. Dzhindzhev, Nikola S. Ohkura, Hiroyuki |
author_sort | Clohisey, Sara M. R. |
collection | PubMed |
description | Little is known about how microtubules are regulated in different cell types during development. EB1 plays a central role in the regulation of microtubule plus ends. It directly binds to microtubule plus ends and recruits proteins which regulate microtubule dynamics and behaviour. We report the identification of Kank, the sole Drosophila orthologue of human Kank proteins, as an EB1 interactor that predominantly localises to embryonic attachment sites between muscle and tendon cells. Human Kank1 was identified as a tumour suppressor and has documented roles in actin regulation and cell polarity in cultured mammalian cells. We found that Drosophila Kank binds EB1 directly and this interaction is essential for Kank localisation to microtubule plus ends in cultured cells. Kank protein is expressed throughout fly development and increases during embryogenesis. In late embryos, it accumulates to sites of attachment between muscle and epidermal cells. A kank deletion mutant was generated. We found that the mutant is viable and fertile without noticeable defects. Further analysis showed that Kank is dispensable for muscle function in larvae. This is in sharp contrast to C. elegans in which the Kank orthologue VAB-19 is required for development by stabilising attachment structures between muscle and epidermal cells. |
format | Online Article Text |
id | pubmed-4159139 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-41591392014-09-12 Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila Clohisey, Sara M. R. Dzhindzhev, Nikola S. Ohkura, Hiroyuki PLoS One Research Article Little is known about how microtubules are regulated in different cell types during development. EB1 plays a central role in the regulation of microtubule plus ends. It directly binds to microtubule plus ends and recruits proteins which regulate microtubule dynamics and behaviour. We report the identification of Kank, the sole Drosophila orthologue of human Kank proteins, as an EB1 interactor that predominantly localises to embryonic attachment sites between muscle and tendon cells. Human Kank1 was identified as a tumour suppressor and has documented roles in actin regulation and cell polarity in cultured mammalian cells. We found that Drosophila Kank binds EB1 directly and this interaction is essential for Kank localisation to microtubule plus ends in cultured cells. Kank protein is expressed throughout fly development and increases during embryogenesis. In late embryos, it accumulates to sites of attachment between muscle and epidermal cells. A kank deletion mutant was generated. We found that the mutant is viable and fertile without noticeable defects. Further analysis showed that Kank is dispensable for muscle function in larvae. This is in sharp contrast to C. elegans in which the Kank orthologue VAB-19 is required for development by stabilising attachment structures between muscle and epidermal cells. Public Library of Science 2014-09-09 /pmc/articles/PMC4159139/ /pubmed/25203404 http://dx.doi.org/10.1371/journal.pone.0106112 Text en © 2014 Clohisey et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Clohisey, Sara M. R. Dzhindzhev, Nikola S. Ohkura, Hiroyuki Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila |
title | Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
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title_full | Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
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title_fullStr | Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
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title_full_unstemmed | Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
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title_short | Kank Is an EB1 Interacting Protein that Localises to Muscle-Tendon Attachment Sites in Drosophila
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title_sort | kank is an eb1 interacting protein that localises to muscle-tendon attachment sites in drosophila |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159139/ https://www.ncbi.nlm.nih.gov/pubmed/25203404 http://dx.doi.org/10.1371/journal.pone.0106112 |
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