SUMOylation Regulates IRF2BP2 Nuclear Localization and Stability

Multi-SUMOylation of IRF2BP2 by UBE2I enhances its importin-{beta}-dependent nuclear localization and contributes to its stability in resting and S-phase cells.

• Why it matters: IRF2BP2’s regulatory mechanisms are unclear, limiting understanding of how this transcriptional cofactor switches between repression and activation through controlled nuclear behavior.
• What they did: The study mapped IRF2BP2 interactions with UBE2I, assessed multi-SUMOylation, tested importin-{beta} dependence and NLS functionality, and examined chromatin accumulation and ubiquitin linkage patterns.
• The result: IRF2BP2 preferentially accumulates in transcriptionally active euchromatin, is not proteasome-degraded, and is stabilized by SUMOylation alongside non-proteolytic K6-linked ubiquitination.

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