Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor
Recognition of apoptotic cells by phagocytes is not fully understood. In C. elegans , the transthyretin-like protein, TTR-52, is secreted by the endoderm and clusters around apoptotic cells, inducing their engulfment through the CED-1/6/7 pathway. During apoptosis, dying cells are swiftly removed by...
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| Veröffentlicht in: | Nature cell biology 2010-07, Vol.12 (7), p.655-664 |
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| creator | Wang, Xiaochen Li, Weida Zhao, Dongfeng Liu, Bin Shi, Yong Chen, Baohui Yang, Hengwen Guo, Pengfei Geng, Xin Shang, Zhihong Peden, Erin Kage-Nakadai, Eriko Mitani, Shohei Xue, Ding |
| description | Recognition of apoptotic cells by phagocytes is not fully understood. In
C. elegans
, the transthyretin-like protein, TTR-52, is secreted by the endoderm and clusters around apoptotic cells, inducing their engulfment through the CED-1/6/7 pathway.
During apoptosis, dying cells are swiftly removed by phagocytes. It is not fully understood how apoptotic cells are recognized by phagocytes. Here we report the identification and characterization of the
Caenorhabditis elegans ttr-52
gene, which encodes a transthyretin-like protein and is required for efficient cell corpse engulfment. The TTR-52 protein is expressed in, and secreted from,
C. elegans
endoderm and clusters around apoptotic cells. Genetic analysis indicates that TTR-52 acts in the cell corpse engulfment pathway mediated by CED-1, CED-6 and CED-7 and affects clustering of the phagocyte receptor CED-1 around apoptotic cells. 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 is therefore 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. |
| doi_str_mv | 10.1038/ncb2068 |
| format | Article |
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C. elegans
, the transthyretin-like protein, TTR-52, is secreted by the endoderm and clusters around apoptotic cells, inducing their engulfment through the CED-1/6/7 pathway.
During apoptosis, dying cells are swiftly removed by phagocytes. It is not fully understood how apoptotic cells are recognized by phagocytes. Here we report the identification and characterization of the
Caenorhabditis elegans ttr-52
gene, which encodes a transthyretin-like protein and is required for efficient cell corpse engulfment. The TTR-52 protein is expressed in, and secreted from,
C. elegans
endoderm and clusters around apoptotic cells. Genetic analysis indicates that TTR-52 acts in the cell corpse engulfment pathway mediated by CED-1, CED-6 and CED-7 and affects clustering of the phagocyte receptor CED-1 around apoptotic cells. 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 is therefore 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.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb2068</identifier><identifier>PMID: 20526330</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/313/1727 ; 631/80/82/23 ; 631/80/86 ; Animals ; Apoptosis ; Apoptosis - genetics ; Apoptosis - physiology ; Biomedical and Life Sciences ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Cancer Research ; Cell Biology ; Cell receptors ; Cells ; Cellular proteins ; Developmental Biology ; Genetic aspects ; Life Sciences ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Models, Biological ; Nematodes ; Phagocytosis ; Physiological aspects ; Proteins ; Stem Cells</subject><ispartof>Nature cell biology, 2010-07, Vol.12 (7), p.655-664</ispartof><rights>Springer Nature Limited 2010</rights><rights>COPYRIGHT 2010 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-ed67fcdb56fcc95d7edc220612f3fd4cf14c550b1951edc2de8d70862f931d453</citedby><cites>FETCH-LOGICAL-c474t-ed67fcdb56fcc95d7edc220612f3fd4cf14c550b1951edc2de8d70862f931d453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20526330$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Xiaochen</creatorcontrib><creatorcontrib>Li, Weida</creatorcontrib><creatorcontrib>Zhao, Dongfeng</creatorcontrib><creatorcontrib>Liu, Bin</creatorcontrib><creatorcontrib>Shi, Yong</creatorcontrib><creatorcontrib>Chen, Baohui</creatorcontrib><creatorcontrib>Yang, Hengwen</creatorcontrib><creatorcontrib>Guo, Pengfei</creatorcontrib><creatorcontrib>Geng, Xin</creatorcontrib><creatorcontrib>Shang, Zhihong</creatorcontrib><creatorcontrib>Peden, Erin</creatorcontrib><creatorcontrib>Kage-Nakadai, Eriko</creatorcontrib><creatorcontrib>Mitani, Shohei</creatorcontrib><creatorcontrib>Xue, Ding</creatorcontrib><title>Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Recognition of apoptotic cells by phagocytes is not fully understood. In
C. elegans
, the transthyretin-like protein, TTR-52, is secreted by the endoderm and clusters around apoptotic cells, inducing their engulfment through the CED-1/6/7 pathway.
During apoptosis, dying cells are swiftly removed by phagocytes. It is not fully understood how apoptotic cells are recognized by phagocytes. Here we report the identification and characterization of the
Caenorhabditis elegans ttr-52
gene, which encodes a transthyretin-like protein and is required for efficient cell corpse engulfment. The TTR-52 protein is expressed in, and secreted from,
C. elegans
endoderm and clusters around apoptotic cells. Genetic analysis indicates that TTR-52 acts in the cell corpse engulfment pathway mediated by CED-1, CED-6 and CED-7 and affects clustering of the phagocyte receptor CED-1 around apoptotic cells. 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 is therefore 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.</description><subject>631/80/313/1727</subject><subject>631/80/82/23</subject><subject>631/80/86</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>Apoptosis - physiology</subject><subject>Biomedical and Life Sciences</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell receptors</subject><subject>Cells</subject><subject>Cellular proteins</subject><subject>Developmental Biology</subject><subject>Genetic aspects</subject><subject>Life Sciences</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Nematodes</subject><subject>Phagocytosis</subject><subject>Physiological aspects</subject><subject>Proteins</subject><subject>Stem Cells</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNptkl2L1DAUhoso7ofiP5CgF6sXXfPRNO3lMq66sCCs43VJk5NO1k7STVJw7vzppsyozCKB5JDzvIfzJqcoXhF8STBrPjjVU1w3T4pTUom6rGrRPl3impeCtfSkOIvxHmNSVVg8L04o5rRmDJ8Wv1YSnA8b2WubbEQwwiBdRCnkPW12AZJ15Wh_AJqCT2AdWq_vSk7RFrSVCSIKoPzgsto75A2Sk5-ST1YhBeMYUb9DaQNodf2xJGjayMGrXYJFBZkLL4pnRo4RXh7O8-L7p-v16kt5-_XzzerqtlSVqFIJuhZG6Z7XRqmWawFa0WyZUMOMrpQhleIc96TlZElpaLTATU1Ny4iuODsvLvZ1s42HGWLqtjYuHUoHfo6dYKymDaE0k28ekfd-Di4313EheNO2vMnQ2z00yBE664zPL6aWkt0VZQS3hOEqU5f_ofLSsLXKOzA23x8J3h8JMpPgZxrkHGN38-3umD04UsHHGMB0U7BbGXYdwd0yFd1hKjL5-uBo7vO3_eX-jEEG3u2BmFNugPDP8uNavwHtqr5U</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Wang, Xiaochen</creator><creator>Li, Weida</creator><creator>Zhao, Dongfeng</creator><creator>Liu, Bin</creator><creator>Shi, Yong</creator><creator>Chen, Baohui</creator><creator>Yang, Hengwen</creator><creator>Guo, Pengfei</creator><creator>Geng, Xin</creator><creator>Shang, Zhihong</creator><creator>Peden, Erin</creator><creator>Kage-Nakadai, Eriko</creator><creator>Mitani, Shohei</creator><creator>Xue, Ding</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20100701</creationdate><title>Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor</title><author>Wang, Xiaochen ; Li, Weida ; Zhao, Dongfeng ; Liu, Bin ; Shi, Yong ; Chen, Baohui ; Yang, Hengwen ; Guo, Pengfei ; Geng, Xin ; Shang, Zhihong ; Peden, Erin ; Kage-Nakadai, Eriko ; Mitani, Shohei ; Xue, Ding</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c474t-ed67fcdb56fcc95d7edc220612f3fd4cf14c550b1951edc2de8d70862f931d453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>631/80/313/1727</topic><topic>631/80/82/23</topic><topic>631/80/86</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - 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Academic</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Xiaochen</au><au>Li, Weida</au><au>Zhao, Dongfeng</au><au>Liu, Bin</au><au>Shi, Yong</au><au>Chen, Baohui</au><au>Yang, Hengwen</au><au>Guo, Pengfei</au><au>Geng, Xin</au><au>Shang, Zhihong</au><au>Peden, Erin</au><au>Kage-Nakadai, Eriko</au><au>Mitani, Shohei</au><au>Xue, Ding</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>12</volume><issue>7</issue><spage>655</spage><epage>664</epage><pages>655-664</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Recognition of apoptotic cells by phagocytes is not fully understood. In
C. elegans
, the transthyretin-like protein, TTR-52, is secreted by the endoderm and clusters around apoptotic cells, inducing their engulfment through the CED-1/6/7 pathway.
During apoptosis, dying cells are swiftly removed by phagocytes. It is not fully understood how apoptotic cells are recognized by phagocytes. Here we report the identification and characterization of the
Caenorhabditis elegans ttr-52
gene, which encodes a transthyretin-like protein and is required for efficient cell corpse engulfment. The TTR-52 protein is expressed in, and secreted from,
C. elegans
endoderm and clusters around apoptotic cells. Genetic analysis indicates that TTR-52 acts in the cell corpse engulfment pathway mediated by CED-1, CED-6 and CED-7 and affects clustering of the phagocyte receptor CED-1 around apoptotic cells. 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 is therefore 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.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>20526330</pmid><doi>10.1038/ncb2068</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/80/313/1727 631/80/82/23 631/80/86 Animals Apoptosis Apoptosis - genetics Apoptosis - physiology Biomedical and Life Sciences Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Cancer Research Cell Biology Cell receptors Cells Cellular proteins Developmental Biology Genetic aspects Life Sciences Membrane Proteins - genetics Membrane Proteins - metabolism Models, Biological Nematodes Phagocytosis Physiological aspects Proteins Stem Cells |
| title | Caenorhabditis elegans transthyretin-like protein TTR-52 mediates recognition of apoptotic cells by the CED-1 phagocyte receptor |
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