Skip to main navigation Skip to search Skip to main content

Dynamic movement of the calcium sensor STIM1 and the calcium channel orai1 in activated T-cells: Puncta and distal caps

  • Valarie A. Barr
  • , Kelsie M. Bernot
  • , Sonal Srikanth
  • , Yousang Gwack
  • , Lakshmi Balagopalan
  • , Carole K. Regan
  • , Daniel J. Helman
  • , Connie L. Sommers
  • , Masatsugu Oh-hora
  • , Anjana Rao
  • , Lawrence E. Samelson

Research output: Contribution to journal › Article › peer-review

Abstract

The proteins STIM1 and Orai1 are the long sought components of the store-operated channels required in T-cell activation. However, little is known about the interaction of these proteins in T-cells after engagement of the T-cell receptor. We found that T-cell receptor engagement caused STIM1 and Orai1 to colocalize in puncta near the site of stimulation and accumulate in a dense structure on the opposite side of the T-cell. FRET measurements showed a close interaction between STIM1 and Orai1 both in the puncta and in the dense cap-like structure. The formation of cap-like structures did not entail rearrangement of the entire endoplasmic reticulum. Cap formation depended on TCR engagement and tyrosine phosphorylation, but not on channel activity or Ca2+ influx. These caps were very dynamic in T-cells activated by contact with superantigen pulsed B-cells and could move from the distal pole to an existing or a newly forming immunological synapse. One function of this cap may be to provide preassembled Ca2+ channel components to existing and newly forming immunological synapses.

Original languageEnglish
Pages (from-to)2802-2817
Number of pages16
JournalMolecular biology of the cell
Volume19
Issue number7
DOIs
Publication statusPublished - Jul 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Dynamic movement of the calcium sensor STIM1 and the calcium channel orai1 in activated T-cells: Puncta and distal caps'. Together they form a unique fingerprint.

Cite this