Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acid Anhydride Hydrolases / genetics
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Acid Anhydride Hydrolases / isolation & purification*
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Acid Anhydride Hydrolases / metabolism*
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Animals
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Animals, Genetically Modified
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Base Sequence / genetics
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Caenorhabditis elegans / cytology
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Caenorhabditis elegans / embryology*
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Caenorhabditis elegans / enzymology
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / isolation & purification
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Caenorhabditis elegans Proteins / metabolism*
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Cell Differentiation / genetics
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Cell Lineage / genetics
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Cell Movement / physiology
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DNA, Complementary / analysis
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DNA, Complementary / genetics
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Disintegrins / metabolism*
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Glycoproteins / metabolism
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Glycosylation
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Gonads / cytology
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Gonads / embryology*
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Gonads / metabolism
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Metalloendopeptidases / metabolism*
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Molecular Sequence Data
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Muscle Cells / metabolism
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Mutation / genetics
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Organogenesis / physiology*
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Stem Cells / cytology
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Stem Cells / metabolism
Substances
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Caenorhabditis elegans Proteins
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DNA, Complementary
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Disintegrins
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Glycoproteins
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MIG-17 protein, C elegans
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Metalloendopeptidases
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Acid Anhydride Hydrolases
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MIG-23 protein, C elegans
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nucleoside-diphosphatase