The nucleoporin RanBP2 has SUMO1 E3 ligase activity
Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 als...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Pichler, Andrea - 1966- [verfasserIn] Gast, Andreas [verfasserIn] Seeler, Jacob S. [verfasserIn] Dejean, Anne [verfasserIn] Melchior, Frauke - 1962- [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
11 January 2002 |
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| Schlagwörter: |
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| Anmerkung: |
Gesehen am 13.03.2023 |
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| Umfang: |
12 |
| Übergeordnetes Werk: |
Enthalten in: Cell - [Cambridge, Mass.] : Cell Press, 1974, 108(2002), 1, Seite 109-120 |
|---|---|
| Übergeordnetes Werk: |
volume:108 ; year:2002 ; number:1 ; pages:109-120 ; extent:12 |
| DOI / URN: |
10.1016/s0092-8674(01)00633-x |
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| Katalog-ID: |
1838989803 |
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| 041 | |a eng | ||
| 100 | 1 | |a Pichler, Andrea |d 1966- |e verfasserin |0 (DE-588)1107797195 |0 (DE-627)863624960 |0 (DE-576)475134044 |4 aut | |
| 245 | 1 | 4 | |a The nucleoporin RanBP2 has SUMO1 E3 ligase activity |c Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior |
| 264 | 1 | |c 11 January 2002 | |
| 300 | |a 12 | ||
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Gesehen am 13.03.2023 | ||
| 520 | |a Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. | ||
| 650 | 4 | |a Animals | |
| 650 | 4 | |a Antibodies | |
| 650 | 4 | |a Antigens, Nuclear | |
| 650 | 4 | |a Autoantigens | |
| 650 | 4 | |a Bacterial Proteins | |
| 650 | 4 | |a Cell Nucleus | |
| 650 | 4 | |a Cytoplasm | |
| 650 | 4 | |a Goats | |
| 650 | 4 | |a GTPase-Activating Proteins | |
| 650 | 4 | |a Ligases | |
| 650 | 4 | |a Luminescent Proteins | |
| 650 | 4 | |a Molecular Chaperones | |
| 650 | 4 | |a Nuclear Pore Complex Proteins | |
| 650 | 4 | |a Nuclear Proteins | |
| 650 | 4 | |a Protein Processing, Post-Translational | |
| 650 | 4 | |a Rabbits | |
| 650 | 4 | |a SUMO-1 Protein | |
| 650 | 4 | |a Ubiquitin-Conjugating Enzymes | |
| 650 | 4 | |a Ubiquitin-Protein Ligases | |
| 650 | 4 | |a Zinc Fingers | |
| 700 | 1 | |a Gast, Andreas |e verfasserin |0 (DE-588)1226448496 |0 (DE-627)1747463841 |4 aut | |
| 700 | 1 | |a Seeler, Jacob S. |e verfasserin |4 aut | |
| 700 | 1 | |a Dejean, Anne |e verfasserin |4 aut | |
| 700 | 1 | |a Melchior, Frauke |d 1962- |e verfasserin |0 (DE-588)1044947144 |0 (DE-627)773153624 |0 (DE-576)370602919 |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Cell |d [Cambridge, Mass.] : Cell Press, 1974 |g 108(2002), 1, Seite 109-120 |h Online-Ressource |w (DE-627)320416127 |w (DE-600)2001951-8 |w (DE-576)090881370 |x 1097-4172 |7 nnns |
| 773 | 1 | 8 | |g volume:108 |g year:2002 |g number:1 |g pages:109-120 |g extent:12 |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ILN_2013 | ||
| 912 | |a ISIL_DE-16-250 | ||
| 912 | |a SYSFLAG_1 | ||
| 912 | |a GBV_KXP | ||
| 912 | |a GBV_ILN_20 | ||
| 912 | |a GBV_ILN_22 | ||
| 912 | |a GBV_ILN_23 | ||
| 912 | |a GBV_ILN_24 | ||
| 912 | |a GBV_ILN_31 | ||
| 912 | |a GBV_ILN_32 | ||
| 912 | |a GBV_ILN_39 | ||
| 912 | |a GBV_ILN_40 | ||
| 912 | |a GBV_ILN_60 | ||
| 912 | |a GBV_ILN_62 | ||
| 912 | |a GBV_ILN_63 | ||
| 912 | |a GBV_ILN_65 | ||
| 912 | |a GBV_ILN_69 | ||
| 912 | |a GBV_ILN_70 | ||
| 912 | |a GBV_ILN_72 | ||
| 912 | |a GBV_ILN_73 | ||
| 912 | |a GBV_ILN_74 | ||
| 912 | |a GBV_ILN_90 | ||
| 912 | |a GBV_ILN_95 | ||
| 912 | |a GBV_ILN_100 | ||
| 912 | |a GBV_ILN_101 | ||
| 912 | |a GBV_ILN_105 | ||
| 912 | |a GBV_ILN_110 | ||
| 912 | |a GBV_ILN_151 | ||
| 912 | |a GBV_ILN_161 | ||
| 912 | |a GBV_ILN_165 | ||
| 912 | |a GBV_ILN_168 | ||
| 912 | |a GBV_ILN_170 | ||
| 912 | |a GBV_ILN_171 | ||
| 912 | |a GBV_ILN_206 | ||
| 912 | |a GBV_ILN_213 | ||
| 912 | |a GBV_ILN_224 | ||
| 912 | |a GBV_ILN_230 | ||
| 912 | |a GBV_ILN_252 | ||
| 912 | |a GBV_ILN_285 | ||
| 912 | |a GBV_ILN_293 | ||
| 912 | |a GBV_ILN_370 | ||
| 912 | |a GBV_ILN_374 | ||
| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_702 | ||
| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
| 912 | |a GBV_ILN_2004 | ||
| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2020 | ||
| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
| 912 | |a GBV_ILN_2026 | ||
| 912 | |a GBV_ILN_2027 | ||
| 912 | |a GBV_ILN_2034 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2112 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
| 912 | |a GBV_ILN_2143 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
| 912 | |a GBV_ILN_2153 | ||
| 912 | |a GBV_ILN_2190 | ||
| 912 | |a GBV_ILN_2336 | ||
| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
| 912 | |a GBV_ILN_2807 | ||
| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4338 | ||
| 912 | |a GBV_ILN_4367 | ||
| 912 | |a GBV_ILN_4393 | ||
| 912 | |a GBV_ILN_4700 | ||
| 951 | |a AR | ||
| 952 | |d 108 |j 2002 |e 1 |h 109-120 |g 12 | ||
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| 982 | |2 2013 |1 01 |x DE-16-250 |8 00 |s s |a hd2002 | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 01 |s s |0 (DE-627)1410508463 |a wissenschaftlicher Artikel (Zeitschrift) | ||
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| 982 | |2 2013 |1 01 |x DE-16-250 |8 03 |s s |a s_12 | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 04 |s p |0 (DE-627)1747463884 |a Gast, Andreas | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 04 |s k |0 (DE-627)1416535500 |a Fakultät für Biowissenschaften | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 04 |s s |0 (DE-627)1410501914 |a Verfasser | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 04 |s s |a pos_2 | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 05 |s p |0 (DE-627)1468249436 |a Melchior, Frauke | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 05 |s k |0 (DE-627)1416822720 |a Extern | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 05 |s s |0 (DE-627)1410501914 |a Verfasser | ||
| 982 | |2 2013 |1 01 |x DE-16-250 |8 05 |s s |a pos_5 | ||
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article:10974172:2002----::hnceprnab2asm13i |
| oclc_num |
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11 January 2002 |
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2002 |
| allfields |
10.1016/s0092-8674(01)00633-x doi (DE-627)1838989803 (DE-599)KXP1838989803 (OCoLC)1389825626 DE-627 ger DE-627 rda eng Pichler, Andrea 1966- verfasserin (DE-588)1107797195 (DE-627)863624960 (DE-576)475134044 aut The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior 11 January 2002 12 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 13.03.2023 Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Seeler, Jacob S. verfasserin aut Dejean, Anne verfasserin aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Enthalten in Cell [Cambridge, Mass.] : Cell Press, 1974 108(2002), 1, Seite 109-120 Online-Ressource (DE-627)320416127 (DE-600)2001951-8 (DE-576)090881370 1097-4172 nnns volume:108 year:2002 number:1 pages:109-120 extent:12 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_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_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_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_2807 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 108 2002 1 109-120 12 2013 01 DE-16-250 4288534097 00 --%%-- --%%-- --%%-- --%%-- l01 13-03-23 2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 |
| spelling |
10.1016/s0092-8674(01)00633-x doi (DE-627)1838989803 (DE-599)KXP1838989803 (OCoLC)1389825626 DE-627 ger DE-627 rda eng Pichler, Andrea 1966- verfasserin (DE-588)1107797195 (DE-627)863624960 (DE-576)475134044 aut The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior 11 January 2002 12 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 13.03.2023 Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Seeler, Jacob S. verfasserin aut Dejean, Anne verfasserin aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Enthalten in Cell [Cambridge, Mass.] : Cell Press, 1974 108(2002), 1, Seite 109-120 Online-Ressource (DE-627)320416127 (DE-600)2001951-8 (DE-576)090881370 1097-4172 nnns volume:108 year:2002 number:1 pages:109-120 extent:12 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_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_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_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_2807 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 108 2002 1 109-120 12 2013 01 DE-16-250 4288534097 00 --%%-- --%%-- --%%-- --%%-- l01 13-03-23 2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 |
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10.1016/s0092-8674(01)00633-x doi (DE-627)1838989803 (DE-599)KXP1838989803 (OCoLC)1389825626 DE-627 ger DE-627 rda eng Pichler, Andrea 1966- verfasserin (DE-588)1107797195 (DE-627)863624960 (DE-576)475134044 aut The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior 11 January 2002 12 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 13.03.2023 Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Seeler, Jacob S. verfasserin aut Dejean, Anne verfasserin aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Enthalten in Cell [Cambridge, Mass.] : Cell Press, 1974 108(2002), 1, Seite 109-120 Online-Ressource (DE-627)320416127 (DE-600)2001951-8 (DE-576)090881370 1097-4172 nnns volume:108 year:2002 number:1 pages:109-120 extent:12 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_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_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_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_2807 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 108 2002 1 109-120 12 2013 01 DE-16-250 4288534097 00 --%%-- --%%-- --%%-- --%%-- l01 13-03-23 2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 |
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10.1016/s0092-8674(01)00633-x doi (DE-627)1838989803 (DE-599)KXP1838989803 (OCoLC)1389825626 DE-627 ger DE-627 rda eng Pichler, Andrea 1966- verfasserin (DE-588)1107797195 (DE-627)863624960 (DE-576)475134044 aut The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior 11 January 2002 12 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 13.03.2023 Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Seeler, Jacob S. verfasserin aut Dejean, Anne verfasserin aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Enthalten in Cell [Cambridge, Mass.] : Cell Press, 1974 108(2002), 1, Seite 109-120 Online-Ressource (DE-627)320416127 (DE-600)2001951-8 (DE-576)090881370 1097-4172 nnns volume:108 year:2002 number:1 pages:109-120 extent:12 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_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_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_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_2807 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 108 2002 1 109-120 12 2013 01 DE-16-250 4288534097 00 --%%-- --%%-- --%%-- --%%-- l01 13-03-23 2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 |
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10.1016/s0092-8674(01)00633-x doi (DE-627)1838989803 (DE-599)KXP1838989803 (OCoLC)1389825626 DE-627 ger DE-627 rda eng Pichler, Andrea 1966- verfasserin (DE-588)1107797195 (DE-627)863624960 (DE-576)475134044 aut The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior 11 January 2002 12 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Gesehen am 13.03.2023 Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers Gast, Andreas verfasserin (DE-588)1226448496 (DE-627)1747463841 aut Seeler, Jacob S. verfasserin aut Dejean, Anne verfasserin aut Melchior, Frauke 1962- verfasserin (DE-588)1044947144 (DE-627)773153624 (DE-576)370602919 aut Enthalten in Cell [Cambridge, Mass.] : Cell Press, 1974 108(2002), 1, Seite 109-120 Online-Ressource (DE-627)320416127 (DE-600)2001951-8 (DE-576)090881370 1097-4172 nnns volume:108 year:2002 number:1 pages:109-120 extent:12 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_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_151 GBV_ILN_161 GBV_ILN_165 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2007 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_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_2807 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 108 2002 1 109-120 12 2013 01 DE-16-250 4288534097 00 --%%-- --%%-- --%%-- --%%-- l01 13-03-23 2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">1838989803</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230710173346.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230313s2002 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/s0092-8674(01)00633-x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)1838989803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)KXP1838989803</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(OCoLC)1389825626</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Pichler, Andrea</subfield><subfield code="d">1966-</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(DE-588)1107797195</subfield><subfield code="0">(DE-627)863624960</subfield><subfield code="0">(DE-576)475134044</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="4"><subfield code="a">The nucleoporin RanBP2 has SUMO1 E3 ligase activity</subfield><subfield code="c">Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">11 January 2002</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">12</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">Gesehen am 13.03.2023</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. 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| standort_str_mv |
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| standort_iln_str_mv |
2013:--%%-- DE-16-250:--%%-- |
| author |
Pichler, Andrea 1966- |
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2013 01 DE-16-250 00 s hd2002 2013 01 DE-16-250 01 s (DE-627)1410508463 wissenschaftlicher Artikel (Zeitschrift) 2013 01 DE-16-250 02 s per_5 2013 01 DE-16-250 03 s s_12 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_2 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_5 The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior Animals Antibodies Antigens, Nuclear Autoantigens Bacterial Proteins Cell Nucleus Cytoplasm Goats GTPase-Activating Proteins Ligases Luminescent Proteins Molecular Chaperones Nuclear Pore Complex Proteins Nuclear Proteins Protein Processing, Post-Translational Rabbits SUMO-1 Protein Ubiquitin-Conjugating Enzymes Ubiquitin-Protein Ligases Zinc Fingers |
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The nucleoporin RanBP2 has SUMO1 E3 ligase activity |
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The nucleoporin RanBP2 has SUMO1 E3 ligase activity Andrea Pichler, Andreas Gast, Jacob S. Seeler, Anne Dejean, Frauke Melchior |
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nucleoporin ranbp2 has sumo1 e3 ligase activity |
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The nucleoporin RanBP2 has SUMO1 E3 ligase activity |
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Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Gesehen am 13.03.2023 |
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Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Gesehen am 13.03.2023 |
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Posttranslational modification with SUMO1 regulates protein/protein interactions, localization, and stability. SUMOylation requires the E1 enzyme Aos1/Uba2 and the E2 enzyme Ubc9. A family of E3-like factors, PIAS proteins, was discovered recently. Here we show that the nucleoporin RanBP2/Nup358 also has SUMO1 E3-like activity. RanBP2 directly interacts with the E2 enzyme Ubc9 and strongly enhances SUMO1-transfer from Ubc9 to the SUMO1 target Sp100. The E3-like activity is contained within a 33 kDa domain of RanBP2 that lacks RING finger motifs and does not resemble PIAS family proteins. Our findings place SUMOylation at the cytoplasmic filaments of the NPC and suggest that, at least for some substrates, modification and nuclear import are linked events. Gesehen am 13.03.2023 |
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