Platelet moesin interacts with PECAM-1 (CD31). (Q47773051)

5 February 2018

title

Platelet moesin interacts with PECAM-1 (CD31). (English)

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5 February 2018

author

Hervé Falet

4

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5 February 2018

Markus Tingart

3

object named as

Markus Tingart

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5 February 2018

author name string

Maria-Andreea Gamulescu

1

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5 February 2018

Kerstin Seifert

2

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5 February 2018

Karin M Hoffmeister

5

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5 February 2018

publication date

1 June 2003

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5 February 2018

published in

Platelets

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5 February 2018

volume

14

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5 February 2018

issue

4

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5 February 2018

page(s)

211-217

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5 February 2018

Mechanisms of actin rearrangements mediating platelet activation

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Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts

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Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes

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Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts

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ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons

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Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway

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Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization

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Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44.

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Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate

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Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins

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ERM proteins in cell adhesion and membrane dynamics

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Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins

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Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association

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Moesin: a member of the protein 4.1-talin-ezrin family of proteins

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Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets

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Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

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Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2

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Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells

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Mechanisms of cold-induced platelet actin assembly

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Platelet endothelial cell adhesion molecule-1 serves as an inhibitory receptor that modulates platelet responses to collagen

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Platelet endothelial cell adhesion molecule-1 is a negative regulator of platelet-collagen interactions

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Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins

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10.1080/0953710031000118830

21 January 2018

Identifiers

DOI

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5 February 2018

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5 February 2018