EWI-2 association with α-actinin regulates T cell immune synapses and HIV viral infection

Mónica Gordón-Alonso, Mónica Sala-Valdés, Vera Rocha-Perugini, Daniel Pérez-Hernández, Soraya López-Martín, Angeles Ursa, Susana Álvarez, Tatiana V. Kolesnikova, Jesús Vázquez, Francisco Sánchez-Madrid, María Yáñez-Mó*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

42 Citations (Scopus)


EWI motif-containing protein 2 (EWI-2) is a member of the Ig superfamily that links tetraspanin-enriched microdomains to the actin cytoskeleton. We found that EWI-2 colocalizes with CD3 and CD81 at the central supramolecular activation cluster of the T cell immune synapse. Silencing of the endogenous expression or overexpression of a cytoplasmic truncated mutant of EWI-2 in T cells increases IL-2 secretion upon Ag stimulation. Mass spectrometry experiments of pull-downs with the C-term intracellular domain of EWI-2 revealed the specific association of EWI-2 with the actin-binding protein α-actinin; this association was regulated by PIP2. α-Actinin regulates the immune synapse formation and is required for efficient T cell activation. We extended these observations to virological synapses induced by HIV and found that silencing of either EWI-2 or a-actinin-4 increased cell infectivity. Our data suggest that the EWI-2-α-actinin complex is involved in the regulation of the actin cytoskeleton at T cell immune and virological synapses, providing a link between membrane microdomains and the formation of polarized membrane structures involved in T cell recognition. Copyright

Original languageEnglish
Pages (from-to)689-700
Number of pages12
JournalJournal of Immunology
Issue number2
Publication statusPublished - 15 Jul 2012
Externally publishedYes


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