Coronin 1 Is Required for Integrin ß2 Translocation in Platelets.
Int J Mol Sci
; 21(1)2020 Jan 05.
Article
en En
| MEDLINE
| ID: mdl-31948107
ABSTRACT
Remodeling of the actin cytoskeleton is one of the critical events that allows platelets to undergo morphological and functional changes in response to receptor-mediated signaling cascades. Coronins are a family of evolutionarily conserved proteins implicated in the regulation of the actin cytoskeleton, represented by the abundant coronins 1, 2, and 3 and the less abundant coronin 7 in platelets, but their functions in these cells are poorly understood. A recent report revealed impaired agonist-induced actin polymerization and cofilin phosphoregulation and altered thrombus formation in vivo as salient phenotypes in the absence of an overt hemostasis defect in vivo in a knockout mouse model of coronin 1. Here we show that the absence of coronin 1 is associated with impaired translocation of integrin ß2 to the platelet surface upon stimulation with thrombin while morphological and functional alterations, including defects in Arp2/3 complex localization and cAMP-dependent signaling, are absent. Our results suggest a large extent of functional overlap among coronins 1, 2, and 3 in platelets, while aspects like integrin ß2 translocation are specifically or predominantly dependent on coronin 1.
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Base de datos:
MEDLINE
Asunto principal:
Plaquetas
/
Cadenas beta de Integrinas
/
Proteínas de Microfilamentos
Idioma:
En
Revista:
Int J Mol Sci
Año:
2020
Tipo del documento:
Article