Modest Interference with Actin Dynamics in Primary T Cell Activation by Antigen Presenting Cells Preferentially Affects Lamellal Signaling

Kole T Roybal, Emily M Mace, Danielle J Clark, Alan D Leard, Andrew Herman, Paul Verkade, Jordan S Orange, Christoph Wülfing

Research output: Contribution to journalArticle (Academic Journal)

5 Citations (Scopus)
311 Downloads (Pure)

Abstract

Dynamic subcellular distributions of signaling system components are critical regulators of cellular signal transduction through their control of molecular interactions. Understanding how signaling activity depends on such distributions and the cellular structures driving them is required for comprehensive insight into signal transduction. In the activation of primary murine T cells by antigen presenting cells (APC) signaling intermediates associate with various subcellular structures, prominently a transient, wide, and actin-associated lamellum extending from an interdigitated T cell:APC interface several micrometers into the T cell. While actin dynamics are well established as general regulators of cellular organization, their role in controlling signaling organization in primary T cell:APC couples and the specific cellular structures driving it is unresolved. Using modest interference with actin dynamics with a low concentration of Jasplakinolide as corroborated by costimulation blockade we show that T cell actin preferentially controls lamellal signaling localization and activity leading downstream to calcium signaling. Lamellal localization repeatedly related to efficient T cell function. This suggests that the transient lamellal actin matrix regulates T cell signaling associations that facilitate T cell activation.

Original languageEnglish
Pages (from-to)e0133231
JournalPLoS ONE
Volume10
Issue number8
Early online date25 Jun 2015
DOIs
Publication statusPublished - 3 Aug 2015

Keywords

  • T cells
  • Actins
  • Calcium signaling
  • Antigen-Presenting cells
  • Cell Signaling
  • Cell membranes
  • Fluorescence recovery after photobleaching
  • Phosphorylation

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