[HTML][HTML] Moesin, the major ERM protein of lymphocytes and platelets, differs from ezrin in its insensitivity to calpain

A Shcherbina, A Bretscher, DM Kenney… - FEBS letters, 1999 - Elsevier
A Shcherbina, A Bretscher, DM Kenney, E Remold-O'Donnell
FEBS letters, 1999Elsevier
The ERM proteins, ezrin, radixin and moesin, provide regulated linkage of the cytoskeleton
with the plasma membrane, particularly in cell surface projections. Ezrin and moesin were
found co-expressed, and radixin was not detected, in human blood lymphocytes, monocytes
and neutrophils. Moesin is the quantitatively dominant ERM protein in these cells and the
only one in platelets. Because Ca2+ signaling pathways involving calpain cleavages are
important in blood cells, we examined ERM protein sensitivity to this protease. A striking …
The ERM proteins, ezrin, radixin and moesin, provide regulated linkage of the cytoskeleton with the plasma membrane, particularly in cell surface projections. Ezrin and moesin were found co-expressed, and radixin was not detected, in human blood lymphocytes, monocytes and neutrophils. Moesin is the quantitatively dominant ERM protein in these cells and the only one in platelets. Because Ca2+ signaling pathways involving calpain cleavages are important in blood cells, we examined ERM protein sensitivity to this protease. A striking difference was discovered: sensitivity of ezrin and resistance of moesin (and radixin) to calpain. In intact stimulated lymphocytes, ezrin was cleaved, while moesin was not, strongly suggesting that differential sensitivity to calpain contributes to specialized functions of these proteins.
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