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. 2016 Oct 26;12(10):e1006400. doi: 10.1371/journal.pgen.1006400

Fig 4. An extended Zasp52 PDZ domain is required for α-actinin binding.

Fig 4

(A) Cartoons of GST-fusion constructs with amino acid length of the Zasp52 part provided. Summary of α-actinin binding ability is shown on the right: +++, normal binding; +, very weak binding;—, no binding. (B) GST pulldown assay. Zasp52-PK and Zasp52-PP interact directly with α-actinin. Zasp52 LIM domains and GST do not interact with α-actinin. (C) GST pulldown assay. Zasp52 PDZ domain interacts weakly with α-actinin, whereas the ZM area does not. (D) GST pulldown assay with a series of truncated proteins. Zasp52-PP, as well as the 143 and 154 amino acid-long Zasp52 proteins bind strongly to α-actinin. However, the 111 amino acid-long Zasp52 protein and Zasp52-PDZ bind weakly to α-actinin.