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Protein Phosphorylation during the Process of Prestalk‐to‐Stalk Conversion in Dictyostelium discoideum
Author(s) -
Maeda Mineko,
Kubohara Yuzuru
Publication year - 1993
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1993.00561.x
Subject(s) - dictyostelium discoideum , stalk , slime mold , protein kinase a , dictyostelium , staurosporine , phosphorylation , microbiology and biotechnology , kinase , mycetozoa , biology , biochemistry , protein phosphorylation , chemistry , gene , horticulture
We have previously shown that 8‐bromo cAMP (Br‐cAMP) efficiently induces prestalk‐to‐stalk conversion in in vitro cultures of the cellular slime mold Dictyostelium discoideum , and that protein kinase A (PKA) plays an important role(s) in the conversion process (Kubohara et al. Exp. Cell Res. vol. 207, pp. 107–114, 1993). In the present study, we analyzed protein phosphorylation during the Br‐cAMP‐induced process, and identified two phosphoproteins, p60 and p40, that were specifically induced (phosphorylated) by Br‐cAMP. The protein kinase inhibitors, staurosporine and K252a, which blocked the Br‐cAMP‐induced stalk cell formation, also inhibited the phosphorylations of these proteins. These results suggest that p60 and p40 may be the target proteins of PKA and thus be involved in the prestalk‐to‐stalk conversion.