Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death

Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 k...
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Gespeichert in:

Autor*in:	Kissil, Joseph L. [verfasserIn] Cohen, Ofer [verfasserIn] Raveh, Tal [verfasserIn] Kimchi, Adi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	1999

Schlagwörter:	anti‐sense apoptosis DAP3 Fas TNF‐γ

Anmerkung:	© European Molecular Biology Organization 1999

Übergeordnetes Werk:	Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 18(1999), 2 vom: 15. Jan., Seite 353-362
Übergeordnetes Werk:	volume:18 ; year:1999 ; number:2 ; day:15 ; month:01 ; pages:353-362

Links:	Volltext

DOI / URN:	10.1093/emboj/18.2.353

Katalog-ID:	SPR057809003

Internformat


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245	1	0	\|a Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
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520			\|a Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level.
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912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
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912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
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912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
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912			\|a GBV_ILN_2088
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912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
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912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2113
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912			\|a GBV_ILN_2119
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912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
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matchkey_str	article:14602075:1999----::tutrfntoaayioaeouinrcnevdrtidpwiheit
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publishDate	1999
allfields	10.1093/emboj/18.2.353 doi (DE-627)SPR057809003 (SPR)18.2.353-e DE-627 ger DE-627 rakwb eng Kissil, Joseph L. verfasserin aut Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213 Cohen, Ofer verfasserin aut Raveh, Tal verfasserin aut Kimchi, Adi verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 2 vom: 15. Jan., Seite 353-362 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:2 day:15 month:01 pages:353-362 https://dx.doi.org/10.1093/emboj/18.2.353 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 1999 2 15 01 353-362
spelling	10.1093/emboj/18.2.353 doi (DE-627)SPR057809003 (SPR)18.2.353-e DE-627 ger DE-627 rakwb eng Kissil, Joseph L. verfasserin aut Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213 Cohen, Ofer verfasserin aut Raveh, Tal verfasserin aut Kimchi, Adi verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 2 vom: 15. Jan., Seite 353-362 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:2 day:15 month:01 pages:353-362 https://dx.doi.org/10.1093/emboj/18.2.353 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 1999 2 15 01 353-362
allfields_unstemmed	10.1093/emboj/18.2.353 doi (DE-627)SPR057809003 (SPR)18.2.353-e DE-627 ger DE-627 rakwb eng Kissil, Joseph L. verfasserin aut Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213 Cohen, Ofer verfasserin aut Raveh, Tal verfasserin aut Kimchi, Adi verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 2 vom: 15. Jan., Seite 353-362 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:2 day:15 month:01 pages:353-362 https://dx.doi.org/10.1093/emboj/18.2.353 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 1999 2 15 01 353-362
allfieldsGer	10.1093/emboj/18.2.353 doi (DE-627)SPR057809003 (SPR)18.2.353-e DE-627 ger DE-627 rakwb eng Kissil, Joseph L. verfasserin aut Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213 Cohen, Ofer verfasserin aut Raveh, Tal verfasserin aut Kimchi, Adi verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 2 vom: 15. Jan., Seite 353-362 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:2 day:15 month:01 pages:353-362 https://dx.doi.org/10.1093/emboj/18.2.353 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 1999 2 15 01 353-362
allfieldsSound	10.1093/emboj/18.2.353 doi (DE-627)SPR057809003 (SPR)18.2.353-e DE-627 ger DE-627 rakwb eng Kissil, Joseph L. verfasserin aut Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213 Cohen, Ofer verfasserin aut Raveh, Tal verfasserin aut Kimchi, Adi verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 2 vom: 15. Jan., Seite 353-362 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:2 day:15 month:01 pages:353-362 https://dx.doi.org/10.1093/emboj/18.2.353 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 18 1999 2 15 01 353-362
language	English
source	Enthalten in The EMBO Journal 18(1999), 2 vom: 15. Jan., Seite 353-362 volume:18 year:1999 number:2 day:15 month:01 pages:353-362
sourceStr	Enthalten in The EMBO Journal 18(1999), 2 vom: 15. Jan., Seite 353-362 volume:18 year:1999 number:2 day:15 month:01 pages:353-362
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	anti‐sense apoptosis DAP3 Fas TNF‐γ
isfreeaccess_bool	false
container_title	The EMBO Journal
authorswithroles_txt_mv	Kissil, Joseph L. @@aut@@ Cohen, Ofer @@aut@@ Raveh, Tal @@aut@@ Kimchi, Adi @@aut@@
publishDateDaySort_date	1999-01-15T00:00:00Z
hierarchy_top_id	266022529
id	SPR057809003
language_de	englisch
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author	Kissil, Joseph L.
spellingShingle	Kissil, Joseph L. misc anti‐sense misc apoptosis misc DAP3 misc Fas misc TNF‐γ Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
authorStr	Kissil, Joseph L.
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topic_title	Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death anti‐sense (dpeaa)DE-He213 apoptosis (dpeaa)DE-He213 DAP3 (dpeaa)DE-He213 Fas (dpeaa)DE-He213 TNF‐γ (dpeaa)DE-He213
topic	misc anti‐sense misc apoptosis misc DAP3 misc Fas misc TNF‐γ
topic_unstemmed	misc anti‐sense misc apoptosis misc DAP3 misc Fas misc TNF‐γ
topic_browse	misc anti‐sense misc apoptosis misc DAP3 misc Fas misc TNF‐γ
format_facet	Elektronische Aufsätze Aufsätze Elektronische Ressource
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title	Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
ctrlnum	(DE-627)SPR057809003 (SPR)18.2.353-e
title_full	Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
author_sort	Kissil, Joseph L.
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author_browse	Kissil, Joseph L. Cohen, Ofer Raveh, Tal Kimchi, Adi
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author-letter	Kissil, Joseph L.
doi_str_mv	10.1093/emboj/18.2.353
author2-role	verfasserin
title_sort	structure–function analysis of an evolutionary conserved protein, dap3, which mediates tnf‐α‐ and fas‐induced cell death
title_auth	Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
abstract	Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. © European Molecular Biology Organization 1999
abstractGer	Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. © European Molecular Biology Organization 1999
abstract_unstemmed	Abstract A novel approach to the isolation of positive mediators of programmed cell death, based on random inactivation of genes by expression of anti sense RNAs, was employed to identify mediators of interferon‐γ‐induced apoptosis. One of the several genes identified is DAP3, which codes for a 46 kDa protein with a potential nucleotide‐binding motif. Structure–function studies of the protein indicate that the intact full‐length protein is required for its ability to induce apoptosis when overexpressed. The N‐terminal 230 amino acids, on the other hand, act in a dominant‐negative fashion. Both of these functions are dependent on the integrity of the nucleotide binding motif. Expression of anti‐sense DAP3 RNA and of the dominant interfering form of DAP3 both protected cells from apoptosis induced by activation of Fas and tumor necrosis factor α (TNF‐α) receptors. Thus, DAP3 is implicated as a positive mediator of these death‐inducing stimuli. It functions downstream of the receptor signaling complex and its death promoting effects depend on caspase activity. In the nematode Caenorhabditis elegans, a potential homolog of DAP3 showing 35% identity and 64% similarity to the human protein was isolated. Overexpression of the nematode DAP3 cDNA in mammalian cells induced cell death, indicating that the protein is conserved at the functional level as well as the structural level. © European Molecular Biology Organization 1999
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title_short	Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death
url	https://dx.doi.org/10.1093/emboj/18.2.353
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author2	Cohen, Ofer Raveh, Tal Kimchi, Adi
author2Str	Cohen, Ofer Raveh, Tal Kimchi, Adi
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doi_str	10.1093/emboj/18.2.353
up_date	2024-10-16T04:51:05.563Z
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Structure–function analysis of an evolutionary conserved protein, DAP3, which mediates TNF‐α‐ and Fas‐induced cell death

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