Coronin 1 is required for integrin β2 translocation in platelets

David R. J. Riley, Jawad S. Khalil, Jean Pieters, Khalid M. Naseem, Francisco Rivero*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

3 Citations (Scopus)
46 Downloads (Pure)


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 β2 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 β2 translocation are specifically or predominantly dependent on coronin 1.

Original languageEnglish
Article number356
Number of pages20
JournalInternational Journal of Molecular Sciences
Issue number1
Publication statusPublished - 5 Jan 2020


  • Actin
  • Arp2/3 complex
  • CAMP
  • Collagen
  • Coronin 1
  • Integrin β2
  • Platelets
  • Prostacyclin
  • Thrombin


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