Platelet moesin interacts with PECAM-1 (CD31).
Platelet activation results information of filopodia and cell spreading by extension of lamellae. Moesin is a member of the ezrin/radixin/moesin (ERM) family of proteins, which localize in cell extensions like filopodia and function as cross-linkers between the actin cytoskeleton and the plasma membrane. Here we investigated whether the adhesion molecule PECAM-1 (CD31) is a membrane-binding partner for moesin in platelets. Our data show that moesin co-immunoprecipitated with PECAM-1 in lysates from thrombin-stimulated, but not resting platelets. Furthermore, PECAM-1 co-localized with moesin at the cell periphery and in filopodia of glass-activated platelets. Our observations suggest that moesin may play a role in platelet adhesion, linking PECAM-1 with the actin cytoskeleton.
Gamulescu
Maria-Andreea
MA
Department of Cardiology and Pneumology, Faculty of Medicine, University of Technology, Aachen, Germany.
Seifert
Kerstin
K
Tingart
Markus
M
Falet
Hervé
H
Hoffmeister
Karin M
KM
D000199:Actins / Q000378:metabolism; D001792:Blood Platelets; D003599:Cytoskeleton / Q000378:metabolism; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism* / Q000502:physiology; D019408:Platelet Endothelial Cell Adhesion Molecule-1 / Q000378:metabolism* / Q000502:physiology; D011233:Precipitin Tests; D011485:Protein Binding; D011554:Pseudopodia / Q000737:chemistry / Q000378:metabolism; D013917:Thrombin
D000199:Actins; D008840:Microfilament Proteins; D019408:Platelet Endothelial Cell Adhesion Molecule-1; C071058:moesin; D013917:Thrombin