Modulated interaction of the ERM protein, moesin, with CD93
نویسندگان
چکیده
منابع مشابه
CD43 interaction with ezrin-radixin-moesin (ERM) proteins regulates T-cell trafficking and CD43 phosphorylation
Cell polarization is a key feature of cell motility, driving cell migration to tissues. CD43 is an abundantly expressed molecule on the T-cell surface that shows distinct localization to the migrating T-cell uropod and the distal pole complex (DPC) opposite the immunological synapse via association with the ezrin-radixin-moesin (ERM) family of actin regulatory proteins. CD43 regulates multiple ...
متن کاملThe actin-binding ERM protein Moesin binds to and stabilizes microtubules at the cell cortex
Ezrin, Radixin, and Moesin (ERM) proteins play important roles in many cellular processes including cell division. Recent studies have highlighted the implications of their metastatic potential in cancers. ERM's role in these processes is largely attributed to their ability to link actin filaments to the plasma membrane. In this paper, we show that the ERM protein Moesin directly binds to micro...
متن کاملERM protein moesin is phosphorylated by advanced glycation end products and modulates endothelial permeability.
Advanced glycation end products (AGEs) accumulated in different pathological conditions have the potent capacity to alter cellular properties that include endothelial structural and functional regulations. The disruption of endothelial barrier integrity may contribute to AGE-induced microangiopathy and macrovasculopathy. Previous studies have shown that AGEs induced the rearrangement of actin a...
متن کاملChemokines induce moesin interaction with ICAM-3.
Activated T lymphocytes are polarized, motile cells. The leading edge of a motile T cell is highly sensitive to chemokines [1, 2]. Chemokines can induce lymphocyte polarization with redistribution of the adhesion molecules, ICAM-1, ICAM-3, CD44, and CD43 to the cell uropod, a membrane protrusion at the end of a migrating lymphocyte opposite the direction of locomotion [3-5]. These events have b...
متن کاملEzrin-radixin-moesin (ERM)-binding phosphoprotein 50 organizes ERM proteins at the apical membrane of polarized epithelia.
Ezrin-radixin-moesin (ERM) proteins regulate the organization and function of specific cortical structures in polarized epithelial cells by connecting filamentous (F)-actin to plasma membrane proteins. The contribution of ERM proteins to these structures depends on a conformational change to an active state in which the C-terminal region interacts with F-actin and the N-terminal domain interact...
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ژورنال
عنوان ژورنال: Immunology
سال: 2005
ISSN: 0019-2805,1365-2567
DOI: 10.1111/j.1365-2567.2005.02120.x