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 language | English |
|---|---|
| Pages (from-to) | 2802-2817 |
| Number of pages | 16 |
| Journal | Molecular biology of the cell |
| Volume | 19 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2008 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology
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