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      The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes.

      Science (New York, N.Y.)

      Animals, pharmacology, Recombinant Fusion Proteins, Proto-Oncogene Proteins c-mos, Protein Synthesis Inhibitors, Progesterone, Phosphorylation, metabolism, enzymology, drug effects, cytology, Oocytes, Mitogen-Activated Protein Kinase 1, Maltose-Binding Proteins, Kinetics, Feedback, Enzyme Activation, Cycloheximide, Cell Cycle, Carrier Proteins

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          Abstract

          Xenopus oocytes convert a continuously variable stimulus, the concentration of the maturation-inducing hormone progesterone, into an all-or-none biological response-oocyte maturation. Here evidence is presented that the all-or-none character of the response is generated by the mitogen-activated protein kinase (MAPK) cascade. Analysis of individual oocytes showed that the response of MAPK to progesterone or Mos was equivalent to that of a cooperative enzyme with a Hill coefficient of at least 35, more than 10 times the Hill coefficient for the binding of oxygen to hemoglobin. The response can be accounted for by the intrinsic ultrasensitivity of the oocyte's MAPK cascade and a positive feedback loop in which the cascade is embedded. These findings provide a biochemical rationale for the all-or-none character of this cell fate switch.

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          9572732

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