TY - JOUR
T1 - One Lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors
AU - Wofsy, Carla
AU - Vonakis, Becky M.
AU - Metzger, Henry
AU - Goldstein, Byron
PY - 1999/7/20
Y1 - 1999/7/20
N2 - In response to antigenic stimuli, the multi-subunit immune recognition receptors become aggregated and then phosphorylated on their cytoplasmic tyrosines. For the clonotypic receptors of B and T cells and for Fc receptors such as the high-affinity receptor for IgE (FcεRI), a Src family kinase initiates this phosphorylation. We ask whether aggregation of the initiating kinase itself is required for signal transduction or whether, alternatively, a single associated kinase molecule can phosphorylate the receptors in an aggregate. We formulate the alternative molecular mechanisms mathematically and compare predictions with experimental findings on FcεRI-bearing cells expressing varying amounts of the transfected Src family kinase Lyn. The data are consistent with the requirement of only a single Lyn molecule per FcεRI aggregate to initiate signaling and are inconsistent with a mechanism requiring more than one Lyn molecule.
AB - In response to antigenic stimuli, the multi-subunit immune recognition receptors become aggregated and then phosphorylated on their cytoplasmic tyrosines. For the clonotypic receptors of B and T cells and for Fc receptors such as the high-affinity receptor for IgE (FcεRI), a Src family kinase initiates this phosphorylation. We ask whether aggregation of the initiating kinase itself is required for signal transduction or whether, alternatively, a single associated kinase molecule can phosphorylate the receptors in an aggregate. We formulate the alternative molecular mechanisms mathematically and compare predictions with experimental findings on FcεRI-bearing cells expressing varying amounts of the transfected Src family kinase Lyn. The data are consistent with the requirement of only a single Lyn molecule per FcεRI aggregate to initiate signaling and are inconsistent with a mechanism requiring more than one Lyn molecule.
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U2 - 10.1073/pnas.96.15.8615
DO - 10.1073/pnas.96.15.8615
M3 - Article
C2 - 10411924
AN - SCOPUS:0033587769
VL - 96
SP - 8615
EP - 8620
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 15
ER -