Charting the Structure and Functional Landscape of the SF3B1 Intrinsically Disordered Region

Phosphorylation of T211, T235, T313, and T328 in the SF3B1 N-terminal 186-341 region shifts 186-341SF3B1 toward more compact, interaction-driven conformational states.

• Why it matters: The SF3B1 NTD is essential for pre-mRNA splicing, yet its disordered structure and how phosphorylation remodelling and RNA binding work remain unclear.
• What they did: Using NMR spectroscopy, SAXS, biochemistry, bioinformatics, and molecular dynamics simulations, the study mapped the conformational landscape of 186-341SF3B1 and tested phosphorylation-dependent changes.
• The result: 186-341SF3B1 remains highly dynamic without stable secondary structure, and it binds RNA transiently and heterogeneously via arginine residues near a conserved tryptophan-centered motif, expanding candidate interactors for splicing regulation.

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