TY - JOUR
T1 - Actin depolymerization transduces the strength of B-cell receptor stimulation
AU - Hao, Shengli
AU - August, Avery
PY - 2005/5
Y1 - 2005/5
N2 - Polymerization of the actin cytoskeleton has been found to be essential for B-cell activation. We show here, however, that stimulation of BCR induces a rapid global actin depolymerization in a BCR signal strength-dependent manner, followed by polarized actin repolymerization. Depolymerization of actin enhances and blocking actin depolymerization inhibits BCR signaling, leading to altered BCR and lipid raft clustering, ERK activation, and transcription factor activation. Furthermore actin depolymerization by itself induces altered lipid raft clustering and ERK activation, suggesting that F-actin may play a role in separating lipid rafts and in setting the threshold for cellular activation.
AB - Polymerization of the actin cytoskeleton has been found to be essential for B-cell activation. We show here, however, that stimulation of BCR induces a rapid global actin depolymerization in a BCR signal strength-dependent manner, followed by polarized actin repolymerization. Depolymerization of actin enhances and blocking actin depolymerization inhibits BCR signaling, leading to altered BCR and lipid raft clustering, ERK activation, and transcription factor activation. Furthermore actin depolymerization by itself induces altered lipid raft clustering and ERK activation, suggesting that F-actin may play a role in separating lipid rafts and in setting the threshold for cellular activation.
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U2 - 10.1091/mbc.E04-10-0881
DO - 10.1091/mbc.E04-10-0881
M3 - Article
C2 - 15728723
AN - SCOPUS:18244397166
SN - 1059-1524
VL - 16
SP - 2275
EP - 2284
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
IS - 5
ER -