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A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation
Stable localization of the signaling complex is essential for the robust morphogenesis of polarized cells. Cell elongation involves molecular signaling centers that coordinately regulate intracellular transport and cytoskeletal structures. In Drosophila bristle elongation, the protein kinase IKKε is...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510591/ https://www.ncbi.nlm.nih.gov/pubmed/26092846 http://dx.doi.org/10.1242/dev.121863 |
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author | Otani, Tetsuhisa Oshima, Kenzi Kimpara, Akiyo Takeda, Michiko Abdu, Uri Hayashi, Shigeo |
author_facet | Otani, Tetsuhisa Oshima, Kenzi Kimpara, Akiyo Takeda, Michiko Abdu, Uri Hayashi, Shigeo |
author_sort | Otani, Tetsuhisa |
collection | PubMed |
description | Stable localization of the signaling complex is essential for the robust morphogenesis of polarized cells. Cell elongation involves molecular signaling centers that coordinately regulate intracellular transport and cytoskeletal structures. In Drosophila bristle elongation, the protein kinase IKKε is activated at the distal tip of the growing bristle and regulates the shuttling movement of recycling endosomes and cytoskeletal organization. However, how the distal tip localization of IKKε is established and maintained during bristle elongation is unknown. Here, we demonstrate that IKKε distal tip localization is regulated by Spindle-F (Spn-F), which is stably retained at the distal tip and functions as an adaptor linking IKKε to cytoplasmic dynein. We found that Javelin-like (Jvl) is a key regulator of Spn-F retention. In jvl mutant bristles, IKKε and Spn-F initially localize to the distal tip but fail to be retained there. In S2 cells, particles that stain positively for Jvl or Spn-F move in a microtubule-dependent manner, whereas Jvl and Spn-F double-positive particles are immobile, indicating that Jvl and Spn-F are transported separately and, upon forming a complex, immobilize each other. These results suggest that polarized transport and selective retention regulate the distal tip localization of the Spn-F–IKKε complex during bristle cell elongation. |
format | Online Article Text |
id | pubmed-4510591 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-45105912015-09-29 A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation Otani, Tetsuhisa Oshima, Kenzi Kimpara, Akiyo Takeda, Michiko Abdu, Uri Hayashi, Shigeo Development Research Article Stable localization of the signaling complex is essential for the robust morphogenesis of polarized cells. Cell elongation involves molecular signaling centers that coordinately regulate intracellular transport and cytoskeletal structures. In Drosophila bristle elongation, the protein kinase IKKε is activated at the distal tip of the growing bristle and regulates the shuttling movement of recycling endosomes and cytoskeletal organization. However, how the distal tip localization of IKKε is established and maintained during bristle elongation is unknown. Here, we demonstrate that IKKε distal tip localization is regulated by Spindle-F (Spn-F), which is stably retained at the distal tip and functions as an adaptor linking IKKε to cytoplasmic dynein. We found that Javelin-like (Jvl) is a key regulator of Spn-F retention. In jvl mutant bristles, IKKε and Spn-F initially localize to the distal tip but fail to be retained there. In S2 cells, particles that stain positively for Jvl or Spn-F move in a microtubule-dependent manner, whereas Jvl and Spn-F double-positive particles are immobile, indicating that Jvl and Spn-F are transported separately and, upon forming a complex, immobilize each other. These results suggest that polarized transport and selective retention regulate the distal tip localization of the Spn-F–IKKε complex during bristle cell elongation. The Company of Biologists 2015-07-01 /pmc/articles/PMC4510591/ /pubmed/26092846 http://dx.doi.org/10.1242/dev.121863 Text en © 2015. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Otani, Tetsuhisa Oshima, Kenzi Kimpara, Akiyo Takeda, Michiko Abdu, Uri Hayashi, Shigeo A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title | A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title_full | A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title_fullStr | A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title_full_unstemmed | A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title_short | A transport and retention mechanism for the sustained distal localization of Spn-F–IKKε during Drosophila bristle elongation |
title_sort | transport and retention mechanism for the sustained distal localization of spn-f–ikkε during drosophila bristle elongation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4510591/ https://www.ncbi.nlm.nih.gov/pubmed/26092846 http://dx.doi.org/10.1242/dev.121863 |
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