Figure 7.
Figure 7. The UCS domain of UNC-45a is critical for NM-II folding. (A) Representative examples of UNC-45a knockout cells transfected with different UNC-45-GFP constructs and treated with MG-132 to induce aggregation of misfolded NM-IIA molecules. F-actin and NM-IIA heavy chains were visualized by phalloidin and antibody staining, respectively. The borders of GFP-positive “rescue cells” are highlighted with yellow lines. Bars, 20 µm. (B) Illustration of domain structures of GFP constructs used in the rescue experiments. (C) Quantification of NM-IIA aggregate formation in UNC-45a knockout cells expressing UNC-45b and various UNC-45a constructs after 4-h treatment with 10 µM MG-132 compound. Data are represented as the percentage of transfected cells positive for both GFP and NM-IIA aggregates; means ± SEM; n = 142 for EGFP, 428 for UNC-45b, 330 for UNC-45a, 410 for ΔTPR, 224 for ΔUCS, and 398 for UCS transfected cells.

The UCS domain of UNC-45a is critical for NM-II folding. (A) Representative examples of UNC-45a knockout cells transfected with different UNC-45-GFP constructs and treated with MG-132 to induce aggregation of misfolded NM-IIA molecules. F-actin and NM-IIA heavy chains were visualized by phalloidin and antibody staining, respectively. The borders of GFP-positive “rescue cells” are highlighted with yellow lines. Bars, 20 µm. (B) Illustration of domain structures of GFP constructs used in the rescue experiments. (C) Quantification of NM-IIA aggregate formation in UNC-45a knockout cells expressing UNC-45b and various UNC-45a constructs after 4-h treatment with 10 µM MG-132 compound. Data are represented as the percentage of transfected cells positive for both GFP and NM-IIA aggregates; means ± SEM; n = 142 for EGFP, 428 for UNC-45b, 330 for UNC-45a, 410 for ΔTPR, 224 for ΔUCS, and 398 for UCS transfected cells.

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