Abstract
Dynamins are large GTPases that act in multiple vesicular trafficking events. We identified 14 loss-of-function alleles of the C. elegans dynamin gene, dyn-1, that are defective in the removal of apoptotic cells. dyn-1 functions in engulfing cells to control the internalization and degradation of apoptotic cells. dyn-1 acts in the genetic pathway composed of ced-7 (ABC transporter), ced-1 (phagocytic receptor), and ced-6 (CED-1's adaptor). DYN-1 transiently accumulates to the surface of pseudopods in a manner dependent on ced-1, ced-6, and ced-7, but not on ced-5, ced-10, or ced-12. Abnormal vesicle structures accumulate in engulfing cells upon dyn-1 inactivation. dyn-1 and ced-1 mutations block the recruitment of intracellular vesicles to pseudopods and phagosomes. We propose that DYN-1 mediates the signaling of the CED-1 pathway by organizing an intracellular vesicle pool and promoting vesicle delivery to phagocytic cups and phagosomes to support pseudopod extension and apoptotic cell degradation.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Amino Acid Sequence
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Animals
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Apoptosis*
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Caenorhabditis elegans / cytology
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Caenorhabditis elegans / embryology
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Caenorhabditis elegans / metabolism
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Caenorhabditis elegans / physiology
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Caenorhabditis elegans / ultrastructure
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Caenorhabditis elegans Proteins / metabolism*
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Conserved Sequence
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Dynamins / chemistry
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Dynamins / genetics
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Dynamins / metabolism*
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Dynamins / physiology
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Dynamins / ultrastructure
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Embryo, Nonmammalian / ultrastructure
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Helminth Proteins / chemistry
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Helminth Proteins / genetics
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Helminth Proteins / metabolism*
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Helminth Proteins / physiology
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Helminth Proteins / ultrastructure
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Membrane Proteins / metabolism*
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Models, Biological
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Molecular Sequence Data
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Mutation
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Phagocytosis
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Signal Transduction*
Substances
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Caenorhabditis elegans Proteins
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Helminth Proteins
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Membrane Proteins
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ced-1 protein, C elegans
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Dyn-1 protein, C elegans
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Dynamins