Disruption of the cortical actin cytoskeleton does not affect store operated Ca2+ channels in human T-cells.
Lymphocyte signaling and activation leads to the influx of extracellular Ca(2+) via the activation of Ca(2+) release activated Ca(2+) (CRAC) channels in the plasma membrane. Activation of CRAC channels occurs following emptying of the endoplasmic reticulum intracellular Ca(2+) stores. One model to explain the coupling of store-emptying to CRAC activation is the secretion-like conformational coupling model. This model proposes that store depletion increases junctions between the endoplasmic reticulum and the plasma membrane in a manner that could be regulated by the cortical actin cytoskeleton. Here, we show that stabilization or depolymerization of the actin cytoskeleton failed to affect CRAC activation. We therefore conclude that rearrangement of the actin cytoskeleton is dispensable for store-operated Ca(2+) entry in T-cells.
Mueller
Philipp
P
Biozentrum, University of Basel, Klingelbergstrasse 70, CH 4056 Basel, Switzerland.
Quintana
Ariel
A
Griesemer
Desiree
D
Hoth
Markus
M
Pieters
Jean
J
D000199:Actins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D015220:Calcium Channels / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism*; D004594:Electrophysiology; D006801:Humans; D019169:Jurkat Cells; D018408:Patch-Clamp Techniques; D013601:T-Lymphocytes / Q000378:metabolism*
D000199:Actins; D015220:Calcium Channels; D002118:Calcium