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Fig. 2. Myoferlin is concentrated at sites of membrane fusion. (A) Confocal images
of differentiating myoblasts, where myoferlin (red) appeared at the membrane,
concentrated at sites of cell-cell contact (arrow and boxed area). (B) Regions
of enhanced myoferlin immunoreactivity (red; and arrowhead) corresponded with
membrane, as they were also positive for caveolin 3 immunoreactivity (green;
arrowhead). Scale bar: 20 µm. (C) The C2A domain of myoferlin was generated
as a GST-fusion protein and tested for calcium-sensitive lipid binding to
3H-labeled vesicles containing 50% phosphotidylcholine and 50%
phosphotidylserine. Binding to C2A required the presence of calcium. Myoferlin
C2A engineered with the mutation I67D showed no phospholipid binding in the
presence of calcium. This mutation is predicted to disrupt the hydrophobic
packing of the ß-strands of the myoferlin C2A domain.
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