Abstract
During apoptosis, the dying cell activates an intrinsic mechanism that quickly dismantles itself. The apoptotic cell corpses are then recognized and removed by neighboring cells or professional phagocytes. How dying cells are degraded after internalization is poorly understood. Here, we report the identification and characterization of unc-108, the Caenorhabditis elegans homolog of the human Rab GTPase 2, as a novel component involved in the degradation of apoptotic cells. unc-108 is expressed and functions in the engulfing cells and is likely to affect the degradation rather than the internalization of cell corpses. Similar to other Rab GTPases, unc-108 also affects endocytosis, acting in the endosomal trafficking from early to late endosome and late endosome to lysosome. UNC-108 co-localizes with RAB-5, RAB-7 and LMP-1 to the phagosome and promotes cell corpse degradation, possibly by mediating phagosome maturation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alleles
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Animals
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Animals, Genetically Modified
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Apoptosis / physiology*
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Caenorhabditis elegans / cytology*
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism*
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Caenorhabditis elegans Proteins / antagonists & inhibitors
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / metabolism*
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Egg Proteins / genetics
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Egg Proteins / metabolism
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Endocytosis / physiology
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Female
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Gene Expression
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Genes, Helminth
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Lysosomes / metabolism
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Membrane Glycoproteins / metabolism
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Mutation
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Phagosomes / metabolism
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RNA Interference
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rab GTP-Binding Proteins / antagonists & inhibitors
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rab GTP-Binding Proteins / genetics
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rab GTP-Binding Proteins / metabolism*
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rab5 GTP-Binding Proteins / metabolism
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rab7 GTP-Binding Proteins
Substances
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Caenorhabditis elegans Proteins
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Egg Proteins
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LMP-1 protein, C elegans
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Membrane Glycoproteins
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rab7 GTP-Binding Proteins
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rab GTP-Binding Proteins
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rab5 GTP-Binding Proteins