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Disruption of the cortical actin cytoskeleton does not affect store operated Ca 2+ channels in human T‐cells
Author(s) -
Mueller Philipp,
Quintana Ariel,
Griesemer Desiree,
Hoth Markus,
Pieters Jean
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.068
Subject(s) - microbiology and biotechnology , endoplasmic reticulum , cytoskeleton , actin cytoskeleton , actin , intracellular , chemistry , actin remodeling of neurons , biophysics , biology , biochemistry , cell
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.