TY - JOUR
T1 - Dynamic movement of the calcium sensor STIM1 and the calcium channel orai1 in activated T-cells
T2 - Puncta and distal caps
AU - Barr, Valarie A.
AU - Bernot, Kelsie M.
AU - Srikanth, Sonal
AU - Gwack, Yousang
AU - Balagopalan, Lakshmi
AU - Regan, Carole K.
AU - Helman, Daniel J.
AU - Sommers, Connie L.
AU - Oh-hora, Masatsugu
AU - Rao, Anjana
AU - Samelson, Lawrence E.
N1 - Copyright:
Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2008/7
Y1 - 2008/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=51349085429&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=51349085429&partnerID=8YFLogxK
U2 - 10.1091/mbc.E08-02-0146
DO - 10.1091/mbc.E08-02-0146
M3 - Article
C2 - 18448669
AN - SCOPUS:51349085429
VL - 19
SP - 2802
EP - 2817
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 7
ER -