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DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair
Epidermal barrier epithelia form a first line of defense against the environment, protecting animals against infection and repairing physical damage. In C. elegans, death-associated protein kinase (DAPK-1) regulates epidermal morphogenesis, innate immunity and wound repair. Combining genetic suppres...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053806/ https://www.ncbi.nlm.nih.gov/pubmed/27661253 http://dx.doi.org/10.7554/eLife.15833 |
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author | Chuang, Marian Hsiao, Tiffany I Tong, Amy Xu, Suhong Chisholm, Andrew D |
author_facet | Chuang, Marian Hsiao, Tiffany I Tong, Amy Xu, Suhong Chisholm, Andrew D |
author_sort | Chuang, Marian |
collection | PubMed |
description | Epidermal barrier epithelia form a first line of defense against the environment, protecting animals against infection and repairing physical damage. In C. elegans, death-associated protein kinase (DAPK-1) regulates epidermal morphogenesis, innate immunity and wound repair. Combining genetic suppressor screens and pharmacological tests, we find that DAPK-1 maintains epidermal tissue integrity through regulation of the microtubule (MT) cytoskeleton. dapk-1 epidermal phenotypes are suppressed by treatment with microtubule-destabilizing drugs and mimicked or enhanced by microtubule-stabilizing drugs. Loss of function in ptrn-1, the C. elegans member of the Patronin/Nezha/CAMSAP family of MT minus-end binding proteins, suppresses dapk-1 epidermal and innate immunity phenotypes. Over-expression of the MT-binding CKK domain of PTRN-1 triggers epidermal and immunity defects resembling those of dapk-1 mutants, and PTRN-1 localization is regulated by DAPK-1. DAPK-1 and PTRN-1 physically interact in co-immunoprecipitation experiments, and DAPK-1 itself undergoes MT-dependent transport. Our results uncover an unexpected interdependence of DAPK-1 and the microtubule cytoskeleton in maintenance of epidermal integrity. DOI: http://dx.doi.org/10.7554/eLife.15833.001 |
format | Online Article Text |
id | pubmed-5053806 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-50538062016-10-11 DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair Chuang, Marian Hsiao, Tiffany I Tong, Amy Xu, Suhong Chisholm, Andrew D eLife Cell Biology Epidermal barrier epithelia form a first line of defense against the environment, protecting animals against infection and repairing physical damage. In C. elegans, death-associated protein kinase (DAPK-1) regulates epidermal morphogenesis, innate immunity and wound repair. Combining genetic suppressor screens and pharmacological tests, we find that DAPK-1 maintains epidermal tissue integrity through regulation of the microtubule (MT) cytoskeleton. dapk-1 epidermal phenotypes are suppressed by treatment with microtubule-destabilizing drugs and mimicked or enhanced by microtubule-stabilizing drugs. Loss of function in ptrn-1, the C. elegans member of the Patronin/Nezha/CAMSAP family of MT minus-end binding proteins, suppresses dapk-1 epidermal and innate immunity phenotypes. Over-expression of the MT-binding CKK domain of PTRN-1 triggers epidermal and immunity defects resembling those of dapk-1 mutants, and PTRN-1 localization is regulated by DAPK-1. DAPK-1 and PTRN-1 physically interact in co-immunoprecipitation experiments, and DAPK-1 itself undergoes MT-dependent transport. Our results uncover an unexpected interdependence of DAPK-1 and the microtubule cytoskeleton in maintenance of epidermal integrity. DOI: http://dx.doi.org/10.7554/eLife.15833.001 eLife Sciences Publications, Ltd 2016-09-23 /pmc/articles/PMC5053806/ /pubmed/27661253 http://dx.doi.org/10.7554/eLife.15833 Text en © 2016, Chuang et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Chuang, Marian Hsiao, Tiffany I Tong, Amy Xu, Suhong Chisholm, Andrew D DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title | DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title_full | DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title_fullStr | DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title_full_unstemmed | DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title_short | DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair |
title_sort | dapk interacts with patronin and the microtubule cytoskeleton in epidermal development and wound repair |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053806/ https://www.ncbi.nlm.nih.gov/pubmed/27661253 http://dx.doi.org/10.7554/eLife.15833 |
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