C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells
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 i...
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Veröffentlicht in: | Development (Cambridge) 2008-03, Vol.135 (6), p.1069-1080 |
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creator | Lu, Qun Zhang, Yan Hu, Tianjing Guo, Pengfei Li, Weida Wang, Xiaochen |
description | 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. |
doi_str_mv | 10.1242/dev.016063 |
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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.</description><identifier>ISSN: 0950-1991</identifier><identifier>EISSN: 1477-9129</identifier><identifier>DOI: 10.1242/dev.016063</identifier><identifier>PMID: 18256195</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>Alleles ; Animals ; Animals, Genetically Modified ; Apoptosis - physiology ; Caenorhabditis elegans ; Caenorhabditis elegans - cytology ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - antagonists & inhibitors ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Egg Proteins - genetics ; Egg Proteins - metabolism ; Endocytosis - physiology ; Female ; Gene Expression ; Genes, Helminth ; Lysosomes - metabolism ; Membrane Glycoproteins - metabolism ; Mutation ; Phagosomes - metabolism ; rab GTP-Binding Proteins - antagonists & inhibitors ; rab GTP-Binding Proteins - genetics ; rab GTP-Binding Proteins - metabolism ; rab5 GTP-Binding Proteins - metabolism ; RNA Interference</subject><ispartof>Development (Cambridge), 2008-03, Vol.135 (6), p.1069-1080</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-dd69fadbc7746db8b8a087d1ef4295844150923554618d490c932f721ea32e543</citedby><cites>FETCH-LOGICAL-c354t-dd69fadbc7746db8b8a087d1ef4295844150923554618d490c932f721ea32e543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18256195$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lu, Qun</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Hu, Tianjing</creatorcontrib><creatorcontrib>Guo, Pengfei</creatorcontrib><creatorcontrib>Li, Weida</creatorcontrib><creatorcontrib>Wang, Xiaochen</creatorcontrib><title>C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells</title><title>Development (Cambridge)</title><addtitle>Development</addtitle><description>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.</description><subject>Alleles</subject><subject>Animals</subject><subject>Animals, Genetically Modified</subject><subject>Apoptosis - physiology</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - cytology</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - antagonists & inhibitors</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Egg Proteins - genetics</subject><subject>Egg Proteins - metabolism</subject><subject>Endocytosis - physiology</subject><subject>Female</subject><subject>Gene Expression</subject><subject>Genes, Helminth</subject><subject>Lysosomes - metabolism</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mutation</subject><subject>Phagosomes - metabolism</subject><subject>rab GTP-Binding Proteins - antagonists & inhibitors</subject><subject>rab GTP-Binding Proteins - genetics</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>rab5 GTP-Binding Proteins - metabolism</subject><subject>RNA Interference</subject><issn>0950-1991</issn><issn>1477-9129</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEURoMotj42_gDJyoUwNe9MllJ8UlCkrkNmcqeNTJsxmSr-e6e04NLV3Zx7-DgIXVAyoUywGw9fE0IVUfwAjanQujCUmUM0JkaSghpDR-gk5w9CCFdaH6MRLZlU1Mgxep5OMLSwcOuM31yFH-avLgNmOGSc4HMTEnjcxIT7JWAPi-S860Nc49hg18Wuj32ocQ1tm8_QUePaDOf7e4re7-_m08di9vLwNL2dFTWXoi-8V6Zxvqq1FspXZVU6UmpPoRHMyFIIKolhXEqhaOmFIbXhrNGMguMMpOCn6Grn7VL83EDu7Srk7QK3hrjJVhM-vFP5L8iI5NywrfF6B9Yp5pygsV0KK5d-LCV2m9gOie0u8QBf7q2bagX-D903HYBiByzDYvk9BLRViG1chNznrQja2FnKpVWDXhn-C1WthE4</recordid><startdate>200803</startdate><enddate>200803</enddate><creator>Lu, Qun</creator><creator>Zhang, Yan</creator><creator>Hu, Tianjing</creator><creator>Guo, Pengfei</creator><creator>Li, Weida</creator><creator>Wang, Xiaochen</creator><general>The Company of Biologists Limited</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200803</creationdate><title>C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells</title><author>Lu, Qun ; Zhang, Yan ; Hu, Tianjing ; Guo, Pengfei ; Li, Weida ; Wang, Xiaochen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-dd69fadbc7746db8b8a087d1ef4295844150923554618d490c932f721ea32e543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Alleles</topic><topic>Animals</topic><topic>Animals, Genetically Modified</topic><topic>Apoptosis - physiology</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - cytology</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - antagonists & inhibitors</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Egg Proteins - genetics</topic><topic>Egg Proteins - metabolism</topic><topic>Endocytosis - physiology</topic><topic>Female</topic><topic>Gene Expression</topic><topic>Genes, Helminth</topic><topic>Lysosomes - metabolism</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mutation</topic><topic>Phagosomes - metabolism</topic><topic>rab GTP-Binding Proteins - antagonists & inhibitors</topic><topic>rab GTP-Binding Proteins - genetics</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>rab5 GTP-Binding Proteins - metabolism</topic><topic>RNA Interference</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Qun</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Hu, Tianjing</creatorcontrib><creatorcontrib>Guo, Pengfei</creatorcontrib><creatorcontrib>Li, Weida</creatorcontrib><creatorcontrib>Wang, Xiaochen</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Development (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Qun</au><au>Zhang, Yan</au><au>Hu, Tianjing</au><au>Guo, Pengfei</au><au>Li, Weida</au><au>Wang, Xiaochen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells</atitle><jtitle>Development (Cambridge)</jtitle><addtitle>Development</addtitle><date>2008-03</date><risdate>2008</risdate><volume>135</volume><issue>6</issue><spage>1069</spage><epage>1080</epage><pages>1069-1080</pages><issn>0950-1991</issn><eissn>1477-9129</eissn><abstract>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.</abstract><cop>England</cop><pub>The Company of Biologists Limited</pub><pmid>18256195</pmid><doi>10.1242/dev.016063</doi><tpages>12</tpages></addata></record> |
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subjects | Alleles Animals Animals, Genetically Modified Apoptosis - physiology Caenorhabditis elegans Caenorhabditis elegans - cytology Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - antagonists & inhibitors Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Egg Proteins - genetics Egg Proteins - metabolism Endocytosis - physiology Female Gene Expression Genes, Helminth Lysosomes - metabolism Membrane Glycoproteins - metabolism Mutation Phagosomes - metabolism rab GTP-Binding Proteins - antagonists & inhibitors rab GTP-Binding Proteins - genetics rab GTP-Binding Proteins - metabolism rab5 GTP-Binding Proteins - metabolism RNA Interference |
title | C. elegans Rab GTPase 2 is required for the degradation of apoptotic cells |
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