Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding
The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occur...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Lin, Xia [verfasserIn] Sun, Baohua [verfasserIn] Liang, Min [verfasserIn] Liang, Yao-Yun [verfasserIn] Gast, Andreas [verfasserIn] Hildebrand, Jeffrey [verfasserIn] Brunicardi, F. Charles [verfasserIn] Melchior, Frauke - 1962- [verfasserIn] Feng, Xin-Hua [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
May 2003 |
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| Anmerkung: |
Gesehen am 05.09.2023 |
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| Umfang: |
8 |
| Übergeordnetes Werk: |
Enthalten in: Molecular cell - [Cambridge, Mass.] : Cell Press, 1997, 11(2003), 5 vom: Mai, Seite 1389-1396 |
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| Übergeordnetes Werk: |
volume:11 ; year:2003 ; number:5 ; month:05 ; pages:1389-1396 ; extent:8 |
| Links: |
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| DOI / URN: |
10.1016/S1097-2765(03)00175-8 |
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| Katalog-ID: |
1858783844 |
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| 100 | 1 | |a Lin, Xia |e verfasserin |0 (DE-588)1300994797 |0 (DE-627)185878459X |4 aut | |
| 245 | 1 | 0 | |a Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding |c Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng |
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| 520 | |a The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. | ||
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10.1016/S1097-2765(03)00175-8 doi (DE-627)1858783844 (DE-599)KXP1858783844 (OCoLC)1425878161 DE-627 ger DE-627 rda eng Lin, Xia verfasserin (DE-588)1300994797 (DE-627)185878459X aut Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng May 2003 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 05.09.2023 The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Sun, Baohua verfasserin aut Liang, Min verfasserin (DE-588)1300999535 (DE-627)1858786657 aut Liang, Yao-Yun verfasserin aut Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Hildebrand, Jeffrey verfasserin aut Brunicardi, F. Charles verfasserin (DE-588)139812350 (DE-627)613783948 (DE-576)188741682 aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Feng, Xin-Hua verfasserin aut Enthalten in Molecular cell [Cambridge, Mass.] : Cell Press, 1997 11(2003), 5 vom: Mai, Seite 1389-1396 Online-Ressource (DE-627)320416097 (DE-600)2001948-8 (DE-576)090881362 1097-4164 nnns volume:11 year:2003 number:5 month:05 pages:1389-1396 extent:8 https://doi.org/10.1016/S1097-2765(03)00175-8 Verlag Resolving-System lizenzpflichtig Volltext https://www.sciencedirect.com/science/article/pii/S1097276503001758 Verlag lizenzpflichtig Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 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_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 11 2003 5 5 1389-1396 8 2013 01 DE-16-250 4372780478 00 --%%-- --%%-- --%%-- --%%-- l01 05-09-23 2013 01 DE-16-250 00 s hd2003 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_8 2013 01 DE-16-250 04 p (DE-627)1747463884 Gast, Andreas 2013 01 DE-16-250 04 k (DE-627)1416535500 Fakultät für Biowissenschaften 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1468249436 Melchior, Frauke 2013 01 DE-16-250 05 k (DE-627)1416822720 Extern 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_8 |
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10.1016/S1097-2765(03)00175-8 doi (DE-627)1858783844 (DE-599)KXP1858783844 (OCoLC)1425878161 DE-627 ger DE-627 rda eng Lin, Xia verfasserin (DE-588)1300994797 (DE-627)185878459X aut Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng May 2003 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 05.09.2023 The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Sun, Baohua verfasserin aut Liang, Min verfasserin (DE-588)1300999535 (DE-627)1858786657 aut Liang, Yao-Yun verfasserin aut Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Hildebrand, Jeffrey verfasserin aut Brunicardi, F. Charles verfasserin (DE-588)139812350 (DE-627)613783948 (DE-576)188741682 aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Feng, Xin-Hua verfasserin aut Enthalten in Molecular cell [Cambridge, Mass.] : Cell Press, 1997 11(2003), 5 vom: Mai, Seite 1389-1396 Online-Ressource (DE-627)320416097 (DE-600)2001948-8 (DE-576)090881362 1097-4164 nnns volume:11 year:2003 number:5 month:05 pages:1389-1396 extent:8 https://doi.org/10.1016/S1097-2765(03)00175-8 Verlag Resolving-System lizenzpflichtig Volltext https://www.sciencedirect.com/science/article/pii/S1097276503001758 Verlag lizenzpflichtig Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 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_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 11 2003 5 5 1389-1396 8 2013 01 DE-16-250 4372780478 00 --%%-- --%%-- --%%-- --%%-- l01 05-09-23 2013 01 DE-16-250 00 s hd2003 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_8 2013 01 DE-16-250 04 p (DE-627)1747463884 Gast, Andreas 2013 01 DE-16-250 04 k (DE-627)1416535500 Fakultät für Biowissenschaften 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1468249436 Melchior, Frauke 2013 01 DE-16-250 05 k (DE-627)1416822720 Extern 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_8 |
| allfields_unstemmed |
10.1016/S1097-2765(03)00175-8 doi (DE-627)1858783844 (DE-599)KXP1858783844 (OCoLC)1425878161 DE-627 ger DE-627 rda eng Lin, Xia verfasserin (DE-588)1300994797 (DE-627)185878459X aut Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng May 2003 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 05.09.2023 The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Sun, Baohua verfasserin aut Liang, Min verfasserin (DE-588)1300999535 (DE-627)1858786657 aut Liang, Yao-Yun verfasserin aut Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Hildebrand, Jeffrey verfasserin aut Brunicardi, F. Charles verfasserin (DE-588)139812350 (DE-627)613783948 (DE-576)188741682 aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Feng, Xin-Hua verfasserin aut Enthalten in Molecular cell [Cambridge, Mass.] : Cell Press, 1997 11(2003), 5 vom: Mai, Seite 1389-1396 Online-Ressource (DE-627)320416097 (DE-600)2001948-8 (DE-576)090881362 1097-4164 nnns volume:11 year:2003 number:5 month:05 pages:1389-1396 extent:8 https://doi.org/10.1016/S1097-2765(03)00175-8 Verlag Resolving-System lizenzpflichtig Volltext https://www.sciencedirect.com/science/article/pii/S1097276503001758 Verlag lizenzpflichtig Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 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_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 11 2003 5 5 1389-1396 8 2013 01 DE-16-250 4372780478 00 --%%-- --%%-- --%%-- --%%-- l01 05-09-23 2013 01 DE-16-250 00 s hd2003 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_8 2013 01 DE-16-250 04 p (DE-627)1747463884 Gast, Andreas 2013 01 DE-16-250 04 k (DE-627)1416535500 Fakultät für Biowissenschaften 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1468249436 Melchior, Frauke 2013 01 DE-16-250 05 k (DE-627)1416822720 Extern 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_8 |
| allfieldsGer |
10.1016/S1097-2765(03)00175-8 doi (DE-627)1858783844 (DE-599)KXP1858783844 (OCoLC)1425878161 DE-627 ger DE-627 rda eng Lin, Xia verfasserin (DE-588)1300994797 (DE-627)185878459X aut Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng May 2003 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 05.09.2023 The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Sun, Baohua verfasserin aut Liang, Min verfasserin (DE-588)1300999535 (DE-627)1858786657 aut Liang, Yao-Yun verfasserin aut Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Hildebrand, Jeffrey verfasserin aut Brunicardi, F. Charles verfasserin (DE-588)139812350 (DE-627)613783948 (DE-576)188741682 aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Feng, Xin-Hua verfasserin aut Enthalten in Molecular cell [Cambridge, Mass.] : Cell Press, 1997 11(2003), 5 vom: Mai, Seite 1389-1396 Online-Ressource (DE-627)320416097 (DE-600)2001948-8 (DE-576)090881362 1097-4164 nnns volume:11 year:2003 number:5 month:05 pages:1389-1396 extent:8 https://doi.org/10.1016/S1097-2765(03)00175-8 Verlag Resolving-System lizenzpflichtig Volltext https://www.sciencedirect.com/science/article/pii/S1097276503001758 Verlag lizenzpflichtig Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 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_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 11 2003 5 5 1389-1396 8 2013 01 DE-16-250 4372780478 00 --%%-- --%%-- --%%-- --%%-- l01 05-09-23 2013 01 DE-16-250 00 s hd2003 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_8 2013 01 DE-16-250 04 p (DE-627)1747463884 Gast, Andreas 2013 01 DE-16-250 04 k (DE-627)1416535500 Fakultät für Biowissenschaften 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1468249436 Melchior, Frauke 2013 01 DE-16-250 05 k (DE-627)1416822720 Extern 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_8 |
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10.1016/S1097-2765(03)00175-8 doi (DE-627)1858783844 (DE-599)KXP1858783844 (OCoLC)1425878161 DE-627 ger DE-627 rda eng Lin, Xia verfasserin (DE-588)1300994797 (DE-627)185878459X aut Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding Xia Lin, Baohua Sun, Min Liang, Yao-Yun Liang, Andreas Gast, Jeffrey Hildebrand, F. Charles Brunicardi, Frauke Melchior, and Xin-Hua Feng May 2003 8 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 05.09.2023 The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Sun, Baohua verfasserin aut Liang, Min verfasserin (DE-588)1300999535 (DE-627)1858786657 aut Liang, Yao-Yun verfasserin aut Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Hildebrand, Jeffrey verfasserin aut Brunicardi, F. Charles verfasserin (DE-588)139812350 (DE-627)613783948 (DE-576)188741682 aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Feng, Xin-Hua verfasserin aut Enthalten in Molecular cell [Cambridge, Mass.] : Cell Press, 1997 11(2003), 5 vom: Mai, Seite 1389-1396 Online-Ressource (DE-627)320416097 (DE-600)2001948-8 (DE-576)090881362 1097-4164 nnns volume:11 year:2003 number:5 month:05 pages:1389-1396 extent:8 https://doi.org/10.1016/S1097-2765(03)00175-8 Verlag Resolving-System lizenzpflichtig Volltext https://www.sciencedirect.com/science/article/pii/S1097276503001758 Verlag lizenzpflichtig Volltext GBV_USEFLAG_U GBV_ILN_2013 ISIL_DE-16-250 SYSFLAG_1 GBV_KXP 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 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_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 11 2003 5 5 1389-1396 8 2013 01 DE-16-250 4372780478 00 --%%-- --%%-- --%%-- --%%-- l01 05-09-23 2013 01 DE-16-250 00 s hd2003 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_9 2013 01 DE-16-250 03 s s_8 2013 01 DE-16-250 04 p (DE-627)1747463884 Gast, Andreas 2013 01 DE-16-250 04 k (DE-627)1416535500 Fakultät für Biowissenschaften 2013 01 DE-16-250 04 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 04 s pos_5 2013 01 DE-16-250 05 p (DE-627)1468249436 Melchior, Frauke 2013 01 DE-16-250 05 k (DE-627)1416822720 Extern 2013 01 DE-16-250 05 s (DE-627)1410501914 Verfasser 2013 01 DE-16-250 05 s pos_8 |
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opposed regulation of corepressor ctbp by sumoylation and pdz binding |
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Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding |
| abstract |
The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Gesehen am 05.09.2023 |
| abstractGer |
The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Gesehen am 05.09.2023 |
| abstract_unstemmed |
The transcription corepressor CtBP is often recruited to the target promoter via interaction with a conserved PxDLS motif in the interacting repressor. In this study, we demonstrate that CtBP1 was SUMOylated and that its SUMOylation profoundly affected its subcellular localization. SUMOylation occurred at a single Lys residue, Lys428, of CtBP1. CtBP2, a close homolog of CtBP1, lacked the SUMOylation site and was not modified by SUMO-1. Mutation of Lys428 into Arg (K428R) shifted CtBP1 from the nucleus to the cytoplasm, while it had little effect on its interaction with the PxDLS motif. Consistent with a change in localization, the K428R mutation abolished the ability of CtBP1 to repress the E-cadherin promoter activity. Notably, SUMOylation of CtBP1 was inhibited by the PDZ domain of nNOS, correlating with the known inhibitory effect of nNOS on the nuclear accumulation of CtBP1. This study identifies SUMOylation as a regulatory mechanism underlying CtBP1-dependent transcriptional repression. Gesehen am 05.09.2023 |
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Opposed regulation of corepressor CtBP by SUMOylation and PDZ binding |
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Sun, Baohua Liang, Min Liang, Yao-Yun Gast, Andreas Hildebrand, Jeffrey Brunicardi, F. Charles Melchior, Frauke 1962- Feng, Xin-Hua |
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