Phosphorylation of Threonine 558 in the Carboxyl-terminal Actin-binding Domain of Moesin by Thrombin Activation of Human Platelets (∗)
F Nakamura, MR Amieva, H Furthmayr - Journal of Biological Chemistry, 1995 - ASBMB
The phosphorylation and localization of the membrane-linking protein moesin was analyzed
during early activation of platelets with thrombin. Activated platelets elaborate filopodia and
spread to assume flat pancake-like shapes, and moesin is localized in filopodia and cell
body. In resting platelets, approximately 25% of moesin molecules are phosphorylated as
shown by metabolic labeling with 32 P i and by isoelectric focusing. Within seconds after
exposure to thrombin, phosphorylation increases, reaching a maximum of 35% labeled …
during early activation of platelets with thrombin. Activated platelets elaborate filopodia and
spread to assume flat pancake-like shapes, and moesin is localized in filopodia and cell
body. In resting platelets, approximately 25% of moesin molecules are phosphorylated as
shown by metabolic labeling with 32 P i and by isoelectric focusing. Within seconds after
exposure to thrombin, phosphorylation increases, reaching a maximum of 35% labeled …