RRC ID 53513
Author Chuang M, Hsiao TI, Tong A, Xu S, Chisholm AD.
Title DAPK interacts with Patronin and the microtubule cytoskeleton in epidermal development and wound repair.
Journal Elife
Abstract 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.
Volume 5
Published 2016-9-23
DOI 10.7554/eLife.15833
PII e15833
PMID 27661253
PMC PMC5053806
MeSH Animals Caenorhabditis elegans / physiology Caenorhabditis elegans Proteins / metabolism* Death-Associated Protein Kinases / metabolism* Epidermis / physiology* Microtubule-Associated Proteins / metabolism* Microtubules / metabolism* Protein Binding Protein Transport Wound Healing*
IF 7.08
Times Cited 8
Resource
C.elegans tm5597 tm2143 tm683 tm773 tm1357 tm3861 tm3124 tm3360 tm4059 tm4957 tm2235