Open AccessThe class I myosin MYO1D binds to lipid and protects against colitis
Author(s) -
William McAlpine,
Kuan-wen Wang,
Jin Huk Choi,
Miguel San Miguel,
Sarah Grace McAlpine,
Jamie Russell,
Sara Ludwig,
Xiaohong Li,
Miao Tang,
Xiaoming Zhan,
Mihwa Choi,
Tao Wang,
Chun Hui Bu,
Anne R. Murray,
Eva Marie Y. Moresco,
Emre E. Turer,
Bruce Beutler
Publication year - 2018
Publication title -
disease models and mechanisms
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.327
H-Index - 83
eISSN - 1754-8411
pISSN - 1754-8403
DOI - 10.1242/dmm.035923
Subject(s) - colitis , myosin , intestinal epithelium , germline , phenotype , mutant , microbiology and biotechnology , brush border , biology , cytoskeleton , intestinal mucosa , chemistry , epithelium , biochemistry , genetics , immunology , gene , medicine , cell , membrane , vesicle
Myosin ID (MYO1D) is a member of the class I myosin family. We screened 48,649 third generation (G3) germline mutant mice derived from N-ethyl-N-nitrosourea-mutagenized grandsires for intestinal homeostasis abnormalities after oral administration of dextran sodium sulfate (DSS). We found and validated mutations in Myo1d as a cause of increased susceptibility to DSS-induced colitis. MYO1D is produced in the intestinal epithelium, and the colitis phenotype is dependent on the nonhematopoietic compartment of the mouse. Moreover, MYO1D appears to couple cytoskeletal elements to lipid in an ATP-dependent manner. These findings demonstrate that MYO1D is needed to maintain epithelial integrity and protect against DSS-induced colitis.
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