An NDPase links ADAM protease glycosylation with organ morphogenesis in C. elegans
| Autor: | Mara Schvarzstein, Yuko Chigira, Kiyoji Nishiwaki, Naoki Hisamoto, Yoshifumi Jigami, Maho Suzuki, Kunihiro Matsumoto, Samir Kumar Roy, Yukihiko Kubota |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
endocrine system
DNA Complementary Glycosylation animal structures Gonad Disintegrins Organogenesis Molecular Sequence Data Morphogenesis medicine.disease_cause Nucleoside-diphosphatase Animals Genetically Modified chemistry.chemical_compound Cell Movement medicine Disintegrin Animals Myocyte Cell Lineage Caenorhabditis elegans Caenorhabditis elegans Proteins Gonads Glycoproteins Muscle Cells Metalloproteinase Mutation Base Sequence biology Stem Cells Metalloendopeptidases Cell Differentiation Cell Biology Acid Anhydride Hydrolases Cell biology carbohydrates (lipids) medicine.anatomical_structure chemistry biology.protein |
| Zdroj: | Nature Cell Biology. 6:31-37 |
| ISSN: | 1476-4679 1465-7392 |
| DOI: | 10.1038/ncb1079 |
| Popis: | In the nematode Caenorhabditis elegans, the gonad acquires two U-shaped arms through the directed migration of its distal tip cells (DTCs), which are located at the tip of the growing gonad arms. A member of the ADAM (a disintegrin and metalloprotease) family, MIG-17, regulates directional migration of DTCs: MIG-17 is synthesized and secreted from the muscle cells of the body wall, and diffuses to the gonad where it is required for DTC migration. The mig-23 mutation causes defective migration of DTCs and interacts genetically with mig-17. Here, we report that mig-23 encodes a membrane-bound nucleoside diphosphatase (NDPase) required for glycosylation and proper localization of MIG-17. Our findings indicate that an NDPase affects organ morphogenesis through glycosylation of the MIG-17 ADAM protease. |
| Databáze: | OpenAIRE |
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