DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair.

Elife

Section of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, San Diego, United States.

Published: September 2016

Epidermal barrier epithelia form a first line of defense against the environment, protecting animals against infection and repairing physical damage. In 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. epidermal phenotypes are suppressed by treatment with microtubule-destabilizing drugs and mimicked or enhanced by microtubule-stabilizing drugs. Loss of function in , the member of the Patronin/Nezha/CAMSAP family of MT minus-end binding proteins, suppresses epidermal and innate immunity phenotypes. Over-expression of the MT-binding CKK domain of PTRN-1 triggers epidermal and immunity defects resembling those of 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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5053806PMC
http://dx.doi.org/10.7554/eLife.15833DOI Listing

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