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Fig. 2. (A) Primary structure of the ERM peptide which reproduces a short sequence located in the C-terminal region of the ERM proteins within the binding site for F-actin (Turunen et al., 1994). An irrelevant peptide having a reversed sequence was used as a control, the control peptide. (B) Fluorescence localization of the ERM peptide in CD8 cells (2 µM, for 3 hours). (C) Moesin distribution in the soluble fraction. Cells were left untreated either stimulated with forskolin or pretreated for 1 or 3 hours with the ERM peptide or preincubated with the control peptide. After homogenization, the amount of protein in the 150,000 g supernatant was determined. Equal amounts of protein (30 µg/lane) were separated by gel electrophoresis and immunoblotted with anti-moesin antibody. Equal loading was confirmed by Coomassie blue staining. Notably, preincubation with the ERM peptide was associated with a strong and time-dependent decrease in moesin abundance in the soluble fraction – an effect similar to, although more potent than, that observed with forskolin treatment.
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