The abstract is read at the publisher; the summary is JClub's.
AlphaFold3-based modeling of the three human GLI-SUFU complexes reveals newly recognized contact interfaces, and binding assays confirm that many interface residues mutated in medulloblastoma and Gorlin syndrome are binding-defective.
- Why it matters: Structural gaps in the GLI-SUFU complex limit interpretation of most patient SUFU missense variants, leaving their clinical significance unclear in cancers and rare congenital syndromes.
- What they did: The authors predicted structures for three human GLI-SUFU complexes and the orthologous Drosophila Ci-Sufu complex using AlphaFold3 and complementary computational analysis, then used site-directed mutagenesis plus GLI-SUFU binding assays to test key interface residues.
- The result: Validated interface residues are linked to familial medulloblastoma and Gorlin syndrome, enabling a structure-function framework to interpret clinically observed SUFU variants and infer mechanisms that tune SUFU repression.
The findingWhy it mattersWhat they didThe result
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