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First published online 6 February 2008
doi: 10.1242/dev.016063

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C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells

Qun Lu^1,3,*, Yan Zhang^2,3,*, Tianjing Hu^3,*, Pengfei Guo³, Weida Li³ and Xiaochen Wang^3,

¹ College of Biological Sciences, China Agricultural University, Beijing 100094, China.
² Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, China.
³ National Institute of Biological Sciences, No. 7 Science Park Road, Zhongguancun Life Science Park, Beijing, 102206, China.

Author for correspondence (e-mail: wangxiaochen{at}nibs.ac.cn)

Accepted 18 January 2008

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.

Key words: C. elegans, Apoptotic cell, Degradation, unc-108, Rab GTPase 2, Endocytosis, Phagosome

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