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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.
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Development ePress online publication date 6 Feb 2008
doi: 10.1242/dev.016063
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Research article
C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells
* Author for correspondence (e-mail: wangxiaochen{at}nibs.ac.cn)
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D. K. Chun, J. M. McEwen, M. Burbea, and J. M. Kaplan
UNC-108/Rab2 Regulates Postendocytic Trafficking in Caenorhabditis elegans
Mol. Biol. Cell,
July 1, 2008;
19(7):
2682 - 2695.
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