Protein Phosphatase 2C Inactivates F-actin Binding of Human Platelet Moesin
نویسندگان
چکیده
منابع مشابه
Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.
Activation of human platelets with thrombin transiently increases phosphorylation at (558)threonine of moesin as determined with phosphorylation state-specific antibodies. This specific modification is completely inhibited by the kinase inhibitor staurosporine and maximally promoted by the phosphatase inhibitor calyculin A, making it possible to purify the two forms of moesin to homogeneity. Bl...
متن کاملProtein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator.
cAMP-dependent phosphorylation activates the cystic fibrosis transmembrane conductance regulator (CFTR) in epithelia. However, the protein phosphatase (PP) that dephosphorylates and inactivates CFTR in airway and intestinal epithelia, two major sites of disease, is not certain. We found that in airway and colonic epithelia, neither okadaic acid nor FK506 prevented inactivation of CFTR when cAMP...
متن کاملGlycoprotein Ib- and actin-binding regions in human platelet actin-binding protein.
Introduction The cytoskeleton in human platelets plays an important role in the dynamic changes that occur during platelet adhesion, shape change and clot retraction. The actin filaments in the cytoskeleton are cross-linked into three-dimensional networks by actin-binding protein (ABP or filamin). The cytoskeleton is linked to the platelet plasma membrane by an association between ABP and a tra...
متن کاملPhosphorylation of platelet actin-binding protein during platelet activation.
In this study we have followed the 32P-labeling of actin-binding protein as a function of platelet activation. Utilizing polyacrylamide-sodium dodecyl sulfate gel electrophoresis to resolve total platelet protein samples, we found 2--3-fold labeling increases in actin-binding protein 30--60 sec after thrombin stimulation. Somewhat larger increases were observed for 40,000 and 20,000 apparent mo...
متن کاملProgestogens regulate endothelial actin cytoskeleton and cell movement via the actin-binding protein moesin.
The endothelial effects of progestogens are poorly investigated. Actin remodeling and cell movement are fundamental for endothelial function and are controlled by the actin-binding protein moesin. In this work, we studied the effects of progesterone and medroxyprogesterone acetate (MPA) on actin remodeling, moesin activation and cell movement in human endothelial cells. Our findings show that p...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.38.26705