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.
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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).
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