SUMOylation of RNA-binding proteins (Li et al. 2004, reviewed in Filosa et al. 2013) alters their interactions with nucleic acids and with proteins. Whereas SUMOylation of HNRNPC decreases its affinity for nucleic acid (ssDNA), SUMOylation of NOP58 is required for binding of snoRNAs. SUMOylation of HNRNPK is required for its coactivation of TP53-dependent transcription.
View original pathway at Reactome.
Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMedEurope PMCScholia
Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; 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
Impens F, Radoshevich L, Cossart P, Ribet D.; ''Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.''; PubMedEurope PMCScholia
Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.; ''Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.''; PubMedEurope PMCScholia
Westman BJ, Lamond AI.; ''A role for SUMOylation in snoRNP biogenesis revealed by quantitative proteomics.''; 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
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
Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMedEurope PMCScholia
Westman BJ, Verheggen C, Hutten S, Lam YW, Bertrand E, Lamond AI.; ''A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates the function of Nop5/Nop58.''; PubMedEurope PMCScholia
Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH, Hay RT.; ''Proteome-wide identification of SUMO2 modification sites.''; PubMedEurope PMCScholia
Kabachinski G, Schwartz TU.; ''The nuclear pore complex--structure and function at a glance.''; PubMedEurope PMCScholia
Matafora V, D'Amato A, Mori S, Blasi F, Bachi A.; ''Proteomics analysis of nucleolar SUMO-1 target proteins upon proteasome inhibition.''; 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
Li T, Evdokimov E, Shen RF, Chao CC, Tekle E, Wang T, Stadtman ER, Yang DC, Chock PB.; ''Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis.''; 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
Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMedEurope PMCScholia
Filosa G, Barabino SM, Bachi A.; ''Proteomics strategies to identify SUMO targets and acceptor sites: a survey of RNA-binding proteins SUMOylation.''; 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
Lee SW, Lee MH, Park JH, Kang SH, Yoo HM, Ka SH, Oh YM, Jeon YJ, Chung CH.; ''SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage.''; PubMedEurope PMCScholia
NOP58 (NOP5) is SUMOylated at lysine-467 and lysine-497 with SUMO1 (Matafora et al. 2009, Westman et al. 2010, Westman and Lamond 2011,Impens et al. 2014). SUMOylation is required for binding of snoRNAs by NOP58.
NOP58 (NOP5) is SUMOylated at lysine-467 and lysine-497 with SUMO2 (Matic et al. 2010, Westman et al. 2010, Westman and Lamond 2011, Hendriks et al. 2014, Impens et al. 2014, Tammsalu et al. 2014). (Two molecules of SUMO2 are shown for each modification in order to represent the oligomeric chains of SUMO2 that are attached to a target protein.) SUMOylation of NOP58 is required for high affinity binding of snoRNAs by NOP58
RANBP2 (NUP358) SUMOylates HNRNPC at lysine-237 of isoform C1 (lysine-250 of the reference isoform C2) with SUMO1 (Vassileva et al. 2004). SUMOylation decreases the interaction of HNRNPC with single-stranded DNA.
CBX4 (Pc2) SUMOylates HNRNPK at lysine-422 with SUMO2 (Li et al. 2004, Lee et al. 2012, Pelisch et al. 2012, Hendriks et al. 2014, Impens et al. 2014, Tammsalu et al. 2014). (Two molecules of SUMO2 are shown in the reaction in order to represent the oligomeric chains of SUMO2 that are attached to a target protein.) PIAS3 also SUMOylates HNRNPK predominantly with SUMO1 (Lee et al. 2012). HNRNPK is SUMOylated in response to DNA damage and SUMOylation is regulated by HIPK2 and CBX4. SUMOylation of HNRNPK is required for coactivation of TP53 (p53) activated transcription. SUMOylation increases the stability of HNRNPK, the nonSUMOylated form of which is normally ubiquinated by HDM2 (Lee et al. 2012).
Try the New WikiPathways
View approved pathways at the new wikipathways.org.Quality Tags
Ontology Terms
Bibliography
History
External references
DataNodes
Annotated Interactions