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

FEBS Letters

Remold-O'Donnell, Eileen¹  Kenney, Dianne M.¹  Bretscher, Anthony²  Shcherbina, Anna¹ 

[1] The Center for Blood Research, Harvard Medical School, 800 Huntington Avenue, Boston, MA 02115, USA;Section on Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853, USA

关键词: Calpain;    Moesin;    Ezrin;    ERM protein;    Platelet;    Lymphocyte;   

DOI  :  10.1016/S0014-5793(98)01674-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown