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Figure 3. Schematic of identified abnormal interactions at the dimer level involving disease-associated K141EHSP22, K141NHSP22, and S135FHSP27. Single interactions were found unchanged (???), moderately increased (???), or greatly increased (???) in comparison with the corresponding wild-type sHSPs in the same interaction. A) K141EHSP22 has moderately increased interactions with itself,
B-Cry, and wtHSP27. B) K141NHSP22 has greatly increased interactions with itself, wtHSP22, and wtHSP27, and moderately increased interaction with
B-Cry. C) S135FHSP27 has moderately increased interaction with wtHSP22. Note that each muHSP22 form has a characteristic, abnormal interaction pattern. That muHSP22 has increased interaction with wtHSP27 and that S135FHSP27 has increased interaction with wtHSP22 and mutations in HSP22 or HSP27 resulting in a similar disease suggest that both mutant proteins may act through the same mechanism.