Cell Corpse Engulfment Mediated by C. elegans Phosphatidylserine Receptor Through CED-5 and CED-12

@article{Wang2003CellCE,
  title={Cell Corpse Engulfment Mediated by C. elegans Phosphatidylserine Receptor Through CED-5 and CED-12},
  author={Xiaochen Wang and Yi-Chun Wu and Valerie Fadok and Ming-Chia Lee and Keiko Gengyo-Ando and Li-Chun Cheng and Duncan Ledwich and Pei-Ken Hsu and Jia-Yun Chen and Bin-Kuan Chou and Peter M. Henson and Shohei Mitani and Ding Xue},
  journal={Science},
  year={2003},
  volume={302},
  pages={1563 - 1566}
}
During apoptosis, phosphatidylserine, which is normally restricted to the inner leaflet of the plasma membrane, is exposed on the surface of apoptotic cells and has been suggested to act as an “eat-me” signal to trigger phagocytosis. It is unclear how phagocytes recognize phosphatidylserine. Recently, a putative phosphatidylserine receptor (PSR) was identified and proposed to mediate recognition of phosphatidylserine and phagocytosis. We report that psr-1, the Caenorhabditis elegans homolog of… 
Two alternative mechanisms that regulate the presentation of apoptotic cell engulfment signal in Caenorhabditis elegans.
TLDR
Observations suggest that phosphatidylserine might be recognized by CED-1 and act as a conserved eat-me signal from nematodes to mammals, and the two different biochemical activities used in somatic cells (ABC transporter) and germ cells (phospholipid scramblase) suggest an increased complexity in the regulation of phosphatidoserine presentation in response to apoptotic signals in different tissues and during different developmental stages.
C. elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor
TLDR
TTR-52 is the first bridging molecule identified in C. elegans that mediates recognition of apoptotic cells by crosslinking the PtdSer 'eat me' signal with the phagocyte receptor CED-1.
Engulfment of Apoptotic Cells in C. elegans Is Mediated by Integrin α/SRC Signaling
A lysine-rich motif in the phosphatidylserine receptor PSR-1 mediates recognition and removal of apoptotic cells
TLDR
A lysine-rich motif in the extracellular domain of PSR-1, the Caenorhabditis elegans PSR, mediates specific phosphatidylserine binding in vitro and clearance of apoptotic cells in vivo, suggesting a mechanism by which PSr-1 activates phagocytosis.
Structural study of TTR-52 reveals the mechanism by which a bridging molecule mediates apoptotic cell engulfment.
TLDR
The structural and functional studies of Caenorhabditis elegans TTR-52, a recently identified bridging molecule that cross-links surface-exposed phosphatidylserine (PtdSer) on apoptotic cells to the CED-1 receptor on phagocytes, reveal the first full-length structure of a bridging substance and the mechanism underlying bridging molecules-mediated apoptotic cell recognition.
C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1
TLDR
The development of an annexin V-based phosphatidylserine labelling method is reported and it is shown that a majority of apoptotic germ cells in Caenorhabditis elegans have surface-exposed phosphatido-serine, indicating that phosphate externalization is a conserved apoptotic event in worms.
SLI-1 Cbl Inhibits the Engulfment of Apoptotic Cells in C. elegans through a Ligase-Independent Function
TLDR
It is proposed that SLI-1 opposes the engulfment of apoptotic cells via a previously unidentified pathway and the RING finger domain of SLI- 1 is not essential to rescue the effects ofSLI-1 deletion on cell migration, suggesting that its role in this process is ubiquitin ligase-independent.
The engulfment process of programmed cell death in caenorhabditis elegans.
TLDR
This work has defined two signal transduction pathways that act redundantly to control engulfment in C. elegans and involves a novel Rac GTPase signaling pathway.
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TLDR
This work reports that ced-5, a gene required for cell-corpse engulfment in the nematode Caenorhabditis elegans, encodes a protein that is similar to the human protein DOCK180 and the Drosophila melanogaster protein Myoblast City, both of which have been implicated in the extension of cell surfaces.
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TLDR
The results suggest that regardless of the receptors engaged on the phagocyte, ingestion does not occur in the absence of phosphatidylserine (PS), and recognition of PS was found to be dependent on the presence of the PS receptor (PSR).
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TLDR
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TLDR
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TLDR
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