Fig. 6
From: Familial STAG2 germline mutation defines a new human cohesinopathy
STAG2 p.Ser327Asn retains binding to WAPL and SGO1 in vitro. a Cartoon diagram of the crystal structure of human STAG2–SCC1, with Ser327 and neighboring residues shown in sticks. b In vitro binding of STAG2–SCC1 to GST-WAPL or GST-Sgo1. GST was used as the negative control. Top and bottom panels show the autoradiograph and Coomassie staining of the binding reactions, respectively. c Quantification of the relative WAPL-binding and SGO1-binding activities of STAG2–SCC1 WT, p.Ser327Asn (Ser327Asn), and Lys330Glu (K330E) (normalized to WT) in b. Mean ± SD, n = 3 independent experiments. For WAPL binding, WT vs. S327N, p = 0.6271, not significant; WT vs. K330E, p < 0.0001. For SGO1 binding, WT vs. S327N, p = 0.0002, p < 0.05; WT vs. K330E, p = 0.0007, p < 0.05. All p-values were based on t-test. d ITC graphs of the binding between pSGO1 and SA2–SCC1 complexes (WT and p.Ser327Asn), with the dissociation constants (K d) indicated
