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. 2010 Jan 26;5(1):e8905. doi: 10.1371/journal.pone.0008905

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Yang et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A. The cue domain of gp78 is responsible for its interaction with htt. Left: Diagram shows GST-gp78c and its truncation mutants used in pull down assay. Right: GST-gp78c and its truncation mutants were incubated with HEK293 cell lysates expressing Nhtt17Q. The Nhtt17Q associated with GST-gp78 was detected with anti-FLAG antibody. GST fusion proteins were stained by ponceau s red. B. The cue domain of gp78 interacts with a region containing the HEAT 2&3 repeats of htt. HEK293 cell lysates expressing various Nhtt truncation mutants containing 17Q were subjected to GST pull down experiment with GST-gp78c and its mutants. Nhtt mutants were detected by immunoblotting. C. Direct interaction of the cue domain of gp78 and the HEAT 2&3 repeats. Recombinant 6His-tagged HEAT 2&3 protein was incubated with GST, GST-cue domain or a GST-Cue domain mutant (Cue-m, see Figure 5A for detailed amino acid changes). Binding of HEAT 2&3 was detected by immunoblotting for 6-His. GST and its fusion proteins were stained by ponceau s red.