SUMOylation processes themselves can be controlled by SUMOylation (reviewed in Wilkinson and Henley 2010). The SUMO E3 ligases PIAS4, RANBP2, and TOPORS are SUMOylated, as is the single SUMO E2 enzyme, UBE2I (UBC9). SUMOylation affects the subcellular location of PIAS4 and TOPORS and affects the activity of PIAS4 and UBE2I.
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Wilkinson KA, Henley JM.; ''Mechanisms, regulation and consequences of protein SUMOylation.''; PubMedEurope PMCScholia
Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMedEurope PMCScholia
Pichler A, Knipscheer P, Saitoh H, Sixma TK, Melchior F.; ''The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.''; PubMedEurope PMCScholia
Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMedEurope PMCScholia
Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMedEurope PMCScholia
Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M.; ''Molecular architecture of the inner ring scaffold of the human nuclear pore complex.''; PubMedEurope PMCScholia
Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMedEurope PMCScholia
Ihara M, Yamamoto H, Kikuchi A.; ''SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4.''; PubMedEurope PMCScholia
Cooper HJ, Tatham MH, Jaffray E, Heath JK, Lam TT, Marshall AG, Hay RT.; ''Fourier transform ion cyclotron resonance mass spectrometry for the analysis of small ubiquitin-like modifier (SUMO) modification: identification of lysines in RanBP2 and SUMO targeted for modification during the E3 autoSUMOylation reaction.''; PubMedEurope PMCScholia
Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMedEurope PMCScholia
Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMedEurope PMCScholia
Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC.; ''Uncovering global SUMOylation signaling networks in a site-specific manner.''; PubMedEurope PMCScholia
Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A.; ''Ubc9 sumoylation regulates SUMO target discrimination.''; PubMedEurope PMCScholia
Lin DH, Stuwe T, Schilbach S, Rundlet EJ, Perriches T, Mobbs G, Fan Y, Thierbach K, Huber FM, Collins LN, Davenport AM, Jeon YE, Hoelz A.; ''Architecture of the symmetric core of the nuclear pore.''; PubMedEurope PMCScholia
Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMedEurope PMCScholia
Weger S, Hammer E, Engstler M.; ''The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation.''; PubMedEurope PMCScholia
Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMedEurope PMCScholia
Pichler A, Gast A, Seeler JS, Dejean A, Melchior F.; ''The nucleoporin RanBP2 has SUMO1 E3 ligase activity.''; PubMedEurope PMCScholia
PIAS4 is SUMOylated at lysine-35 with SUMO1 (Ihara et al. 2005). SUMOylation of PIAS4 at lysine-35 decreases its localization with PML. SUMOylated PIAS4 is able to increase SUMOylation and transcriptional activity of TCF4.
UBE2I (UBC9) is SUMOylated at lysine-14 with SUMO1 (Knipscheer et al. 2008). SUMOylation alters the target specificity of UBE2I, decreasing its SUMOylation activity towards RanGAP1 and increasing it towards SP100.
RANBP2 SUMOylates RANBP2 at lysine-2592, lysine-2650, and lysine-2723 with SUMO1 (Pichler et al. 2002, Pichler et al. 2004, Cooper et al. 2005). RANBP2 does not resemble HECT or RING type SUMO E3 ligases and instead uses hydrophobic interactions with UBE2I (UBC9) to catalyze SUMOylation.
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