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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-09-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/15833 |
| _version_ | 1818018985519611904 |
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| author | Marian Chuang Tiffany I Hsiao Amy Tong Suhong Xu Andrew D Chisholm |
| author_facet | Marian Chuang Tiffany I Hsiao Amy Tong Suhong Xu Andrew D Chisholm |
| author_sort | Marian Chuang |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-14T07:47:03Z |
| format | Article |
| id | doaj.art-52f0f1987ef14fb5b308987406756a73 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-14T07:47:03Z |
| publishDate | 2016-09-01 |
| publisher | eLife Sciences Publications Ltd |
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| series | eLife |
| spelling | doaj.art-52f0f1987ef14fb5b308987406756a732022-12-22T02:05:19ZengeLife Sciences Publications LtdeLife2050-084X2016-09-01510.7554/eLife.15833DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repairMarian Chuang0Tiffany I Hsiao1Amy Tong2Suhong Xu3Andrew D Chisholm4https://orcid.org/0000-0001-5091-0537Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United StatesSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United StatesSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United StatesSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United StatesSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United StatesEpidermal 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.https://elifesciences.org/articles/15833PatroninCAMSAPepithelial cellssuppression |
| spellingShingle | Marian Chuang Tiffany I Hsiao Amy Tong Suhong Xu Andrew D Chisholm DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair eLife Patronin CAMSAP epithelial cells suppression |
| 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 | Patronin CAMSAP epithelial cells suppression |
| url | https://elifesciences.org/articles/15833 |
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