Premium
Moesin, the major ERM protein of lymphocytes and platelets, differs from ezrin in its insensitivity to calpain
Author(s) -
Shcherbina Anna,
Bretscher Anthony,
Kenney Dianne M.,
Remold-O'Donnell Eileen
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01674-3
Subject(s) - moesin , ezrin , radixin , microbiology and biotechnology , calpain , cytoskeleton , platelet , chemistry , biology , cell , immunology , biochemistry , enzyme
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 Ca 2+ 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.