TY - JOUR
T1 - Cells respond to and bind countin, a component of a multisubunit cell number counting factor
AU - Gao, Tong
AU - Ehrenman, Karen
AU - Tang, Lei
AU - Leippe, Matthias
AU - Brock, Debra A.
AU - Gomer, Richard H.
PY - 2002/9/6
Y1 - 2002/9/6
N2 - In Dictyostelium discoideum counting factor (CF), a secreted ∼450-kDa complex of polypeptides, inhibits group and fruiting body size. When the gene encoding countin (a component of CF) was disrupted, cells formed large groups. We find that recombinant countin causes developing cells to form small groups, with an EC50 of ∼3 ng/ml, and affects cAMP signal transduction in the same manner as semipurified CF. Recombinant countin increases cell motility, decreases cell-cell adhesion, and regulates gene expression in a manner similar to the effect of CF. However, countin does not decrease adhesion or group size to the extent that semipurified CF does. A 1-min exposure of developing cells to countin causes an increase in F-actin polymerization and myosin phosphorylation and a decrease in myosin polymerization, suggesting that countin activates a rapid signal transduction pathway. 125I-Labeled countin has countin bioactivity, and binding experiments suggest that vegetative and developing cells have ∼53 cell-surface sites that bind countin with a KD of ∼1.5 ng/ml or 60 pM. We hypothesize that countin regulates cell development through the same pathway as CF and that other proteins within the complex may modify the activity of countin and/or have independent size-regulating activities.
AB - In Dictyostelium discoideum counting factor (CF), a secreted ∼450-kDa complex of polypeptides, inhibits group and fruiting body size. When the gene encoding countin (a component of CF) was disrupted, cells formed large groups. We find that recombinant countin causes developing cells to form small groups, with an EC50 of ∼3 ng/ml, and affects cAMP signal transduction in the same manner as semipurified CF. Recombinant countin increases cell motility, decreases cell-cell adhesion, and regulates gene expression in a manner similar to the effect of CF. However, countin does not decrease adhesion or group size to the extent that semipurified CF does. A 1-min exposure of developing cells to countin causes an increase in F-actin polymerization and myosin phosphorylation and a decrease in myosin polymerization, suggesting that countin activates a rapid signal transduction pathway. 125I-Labeled countin has countin bioactivity, and binding experiments suggest that vegetative and developing cells have ∼53 cell-surface sites that bind countin with a KD of ∼1.5 ng/ml or 60 pM. We hypothesize that countin regulates cell development through the same pathway as CF and that other proteins within the complex may modify the activity of countin and/or have independent size-regulating activities.
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U2 - 10.1074/jbc.M203075200
DO - 10.1074/jbc.M203075200
M3 - Article
C2 - 12070154
AN - SCOPUS:0037031889
SN - 0021-9258
VL - 277
SP - 32596
EP - 32605
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -