The role of receptor internalization in CD95 signaling
Activation of the cell surface CD95 receptor triggers a cascade of signaling events, including assembly of the death‐inducing signaling complex (DISC), that culminate in cellular apoptosis. In this study, we demonstrate a general requirement of receptor internalization for CD95 ligand‐mediated DISC...
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| Veröffentlicht in: | The EMBO journal 2006-03, Vol.25 (5), p.1009-1023 |
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| creator | Lee, Kyeong-Hee Feig, Christine Tchikov, Vladimir Schickel, Robert Hallas, Cora Schütze, Stefan Peter, Marcus E Chan, Andrew C |
| description | Activation of the cell surface CD95 receptor triggers a cascade of signaling events, including assembly of the death‐inducing signaling complex (DISC), that culminate in cellular apoptosis. In this study, we demonstrate a general requirement of receptor internalization for CD95 ligand‐mediated DISC amplification, caspase activation and apoptosis in type I cells. Recruitment of DISC components to the activated receptor predominantly occurs after the receptor has moved into an endosomal compartment and blockade of CD95 internalization impairs DISC formation and apoptosis. In contrast, CD95 ligand stimulation of cells unable to internalize CD95 results in activation of proliferative Erk and NF‐κB signaling pathways. Hence, the subcellular localization and internalization pathways of CD95 play important roles in controlling activation of distinct signaling cascades to determine divergent cellular fates. |
| doi_str_mv | 10.1038/sj.emboj.7601016 |
| format | Article |
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In this study, we demonstrate a general requirement of receptor internalization for CD95 ligand‐mediated DISC amplification, caspase activation and apoptosis in type I cells. Recruitment of DISC components to the activated receptor predominantly occurs after the receptor has moved into an endosomal compartment and blockade of CD95 internalization impairs DISC formation and apoptosis. In contrast, CD95 ligand stimulation of cells unable to internalize CD95 results in activation of proliferative Erk and NF‐κB signaling pathways. Hence, the subcellular localization and internalization pathways of CD95 play important roles in controlling activation of distinct signaling cascades to determine divergent cellular fates.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7601016</identifier><identifier>PMID: 16498403</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Apoptosis ; Caspase 8 ; Caspases - metabolism ; Cells ; Clathrin - metabolism ; Death Domain Receptor Signaling Adaptor Proteins ; EMBO19 ; EMBO37 ; Endocytosis ; endosomes ; Endosomes - metabolism ; Enzyme Activation ; Fas Ligand Protein ; fas Receptor - metabolism ; Fas-Associated Death Domain Protein ; Humans ; Membrane Glycoproteins - metabolism ; Mitogen-Activated Protein Kinases - metabolism ; Neurons ; NF-kappa B - metabolism ; Signal Transduction ; Subcellular Fractions ; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism ; Tumor Necrosis Factors - metabolism</subject><ispartof>The EMBO journal, 2006-03, Vol.25 (5), p.1009-1023</ispartof><rights>European Molecular Biology Organization 2006</rights><rights>Copyright © 2006 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Mar 8, 2006</rights><rights>Copyright © 2006, European Molecular Biology Organization 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6176-2146e788dc407ec9c33ff52e099cb612f0be620787cbebc63b121fb28162208e3</citedby><cites>FETCH-LOGICAL-c6176-2146e788dc407ec9c33ff52e099cb612f0be620787cbebc63b121fb28162208e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1409734/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1409734/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,41096,42165,45550,45551,46384,46808,51551,53766,53768</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/sj.emboj.7601016$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16498403$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Kyeong-Hee</creatorcontrib><creatorcontrib>Feig, Christine</creatorcontrib><creatorcontrib>Tchikov, Vladimir</creatorcontrib><creatorcontrib>Schickel, Robert</creatorcontrib><creatorcontrib>Hallas, Cora</creatorcontrib><creatorcontrib>Schütze, Stefan</creatorcontrib><creatorcontrib>Peter, Marcus E</creatorcontrib><creatorcontrib>Chan, Andrew C</creatorcontrib><title>The role of receptor internalization in CD95 signaling</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Activation of the cell surface CD95 receptor triggers a cascade of signaling events, including assembly of the death‐inducing signaling complex (DISC), that culminate in cellular apoptosis. In this study, we demonstrate a general requirement of receptor internalization for CD95 ligand‐mediated DISC amplification, caspase activation and apoptosis in type I cells. Recruitment of DISC components to the activated receptor predominantly occurs after the receptor has moved into an endosomal compartment and blockade of CD95 internalization impairs DISC formation and apoptosis. In contrast, CD95 ligand stimulation of cells unable to internalize CD95 results in activation of proliferative Erk and NF‐κB signaling pathways. Hence, the subcellular localization and internalization pathways of CD95 play important roles in controlling activation of distinct signaling cascades to determine divergent cellular fates.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Apoptosis</subject><subject>Caspase 8</subject><subject>Caspases - metabolism</subject><subject>Cells</subject><subject>Clathrin - metabolism</subject><subject>Death Domain Receptor Signaling Adaptor Proteins</subject><subject>EMBO19</subject><subject>EMBO37</subject><subject>Endocytosis</subject><subject>endosomes</subject><subject>Endosomes - metabolism</subject><subject>Enzyme Activation</subject><subject>Fas Ligand Protein</subject><subject>fas Receptor - metabolism</subject><subject>Fas-Associated Death Domain Protein</subject><subject>Humans</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Neurons</subject><subject>NF-kappa B - metabolism</subject><subject>Signal Transduction</subject><subject>Subcellular Fractions</subject><subject>Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism</subject><subject>Tumor Necrosis Factors - metabolism</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkUtv1DAUhS1ERYfCnhWKWLDL4GsnfmyQ6NBOaYfHosDSStybqUMmHuxMofx6PGTUBxJiZdn-zvHxPYQ8AzoFytWr2E5xVft2KgUFCuIBmUAhaM6oLB-SCWUC8gKU3iePY2wppaWS8Ijsgyi0KiifEHF-iVnwHWa-yQJaXA8-ZK4fMPRV535Vg_N92mezt7rMoltuT_vlE7LXVF3Ep7v1gHw-PjqfneSLj_N3szeL3AqQImcpDUqlLmxBJVptOW-akiHV2tYCWENrFCmskrbG2gpeA4OmZgoEY1QhPyCvR9_1pl7hhcV-CFVn1sGtqnBtfOXM_ZveXZqlvzJQUC15kQxe7gyC_77BOJiVixa7rurRb6IRUjIOsAVf_AW2frOdQTSgSybTRCFBdIRs8DEGbG6SADXbRkxszZ9GzK6RJHl-9we3gl0FCdAj8MN1eP1fQ3P0_vD01hxGbUyyfonhTuh_B8pHjYsD_rx5rwrf0jC4LM3XD3PzZXHGTj7NwQj-G2anuUA</recordid><startdate>20060308</startdate><enddate>20060308</enddate><creator>Lee, Kyeong-Hee</creator><creator>Feig, Christine</creator><creator>Tchikov, Vladimir</creator><creator>Schickel, Robert</creator><creator>Hallas, Cora</creator><creator>Schütze, Stefan</creator><creator>Peter, Marcus E</creator><creator>Chan, Andrew C</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><scope>BSCLL</scope><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</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>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060308</creationdate><title>The role of receptor internalization in CD95 signaling</title><author>Lee, Kyeong-Hee ; Feig, Christine ; Tchikov, Vladimir ; Schickel, Robert ; Hallas, Cora ; Schütze, Stefan ; Peter, Marcus E ; Chan, Andrew C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6176-2146e788dc407ec9c33ff52e099cb612f0be620787cbebc63b121fb28162208e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adaptor Proteins, Signal Transducing - 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| subjects | Adaptor Proteins, Signal Transducing - metabolism Apoptosis Caspase 8 Caspases - metabolism Cells Clathrin - metabolism Death Domain Receptor Signaling Adaptor Proteins EMBO19 EMBO37 Endocytosis endosomes Endosomes - metabolism Enzyme Activation Fas Ligand Protein fas Receptor - metabolism Fas-Associated Death Domain Protein Humans Membrane Glycoproteins - metabolism Mitogen-Activated Protein Kinases - metabolism Neurons NF-kappa B - metabolism Signal Transduction Subcellular Fractions Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism Tumor Necrosis Factors - metabolism |
| title | The role of receptor internalization in CD95 signaling |
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