Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor.
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TTR-52 recognizes surface-exposed phosphatidylserine (PtdSer) in vivo and binds to both PtdSer and the extracellular domain of CED-1 in vitro
"TTR-52 recognizes surface-exposed phosphatidylserine (PtdSer) in vivo and binds to both PtdSer and the extracellular domain of CED-1 in vitro"
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mediates recognition of apoptotic cells by crosslinking the PtdSer 'eat me' signal with the phagocyte receptor CED-1
"mediates recognition of apoptotic cells by crosslinking the PtdSer 'eat me' signal with the phagocyte receptor CED-1"
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The TTR-52 protein is expressed in, and secreted from, C. elegans endoderm and clusters around apoptotic cells
"The TTR-52 protein is expressed in, and secreted from, C. elegans endoderm and clusters around apoptotic cells"
Structural study of TTR-52 reveals the mechanism by which a bridging molecule mediates apoptotic cell engulfment.
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CED-1 binds TTR-52 through its N-terminal EMI domain and that the hydrophobic region of the TTR-52 C terminus is involved in this interaction
"CED-1 binds TTR-52 through its N-terminal EMI domain and that the hydrophobic region of the TTR-52 C terminus is involved in this interaction"
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TTR-52 is proposed to bind PtdSer via an "ion-mediating" PtdSer-binding mode
"TTR-52 is proposed to bind PtdSer via an "ion-mediating" PtdSer-binding mode"
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TTR-52 forms dimers, and its dimerization is important for its function in vivo
"TTR-52 forms dimers, and its dimerization is important for its function in vivo"
C. elegans secreted lipid-binding protein NRF-5 mediates PS appearance on phagocytes for cell corpse engulfment.
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NRF-5 associates with TTR-52, binds PS, and displays lipid transfer activity in vitro
"NRF-5 associates with TTR-52, binds PS, and displays lipid transfer activity in vitro"
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NRF-5 may act with CED-7 and TTR-52 to mediate PS transfer from apoptotic cells to engulfing cells
"NRF-5 may act with CED-7 and TTR-52 to mediate PS transfer from apoptotic cells to engulfing cells"
CED-1, CED-7, and TTR-52 regulate surface phosphatidylserine expression on apoptotic and phagocytic cells.
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CED-7 and TTR-52 may promote the efflux of PS from apoptotic cells through the generation of extracellular PS vesicles
"CED-7 and TTR-52 may promote the efflux of PS from apoptotic cells through the generation of extracellular PS vesicles"
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indicating that PS-binding TTR-52 also associates with extracellular PS vesicles and may participate in the generation of these PS vesicles
"indicating that PS-binding TTR-52 also associates with extracellular PS vesicles and may participate in the generation of these PS vesicles"
Caspase-mediated activation of Caenorhabditis elegans CED-8 promotes apoptosis and phosphatidylserine externalization.
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only mildly enhanced the corpse engulfment defect of the ced-1, ced-6, ced-7 or ttr-52 mutants at the L1 larval stage
"only mildly enhanced the corpse engulfment defect of the ced-1, ced-6, ced-7 or ttr-52 mutants at the L1 larval stage"
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mainly act through the ced-1, ced-6, ced-7 and ttr-52 engulfment pathway to promote phagocytosis
"mainly act through the ced-1, ced-6, ced-7 and ttr-52 engulfment pathway to promote phagocytosis"
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods