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Endogenous substrates for protein kinases in Coprinus macrorhizus
Biochimica Et Biophysica Acta
|March 5, 1981
Summary
Cyclic AMP influences protein phosphorylation in Coprinus macrorhizus mycelia. It stimulates two proteins (A and B) and inhibits one (Protein C), with rapid phosphorylation observed.
Area of Science:
- Biochemistry
- Mycology
- Cellular Biology
Background:
- Cellular signaling pathways are crucial for fungal development.
- Protein phosphorylation is a key regulatory mechanism in cellular processes.
Purpose of the Study:
- To investigate the effect of cyclic AMP on protein phosphorylation in Coprinus macrorhizus mycelia.
- To identify and characterize proteins whose phosphorylation is modulated by cyclic AMP.
Main Methods:
- Mycelia of Coprinus macrorhizus (strain Fisc) were subjected to varying cyclic AMP concentrations.
- Protein phosphorylation levels were assessed using gel electrophoresis in the presence of sodium dodecyl sulfate (SDS).
- Molecular weights of affected proteins were determined.
Main Results:
- Cyclic AMP (cAMP) stimulated the phosphorylation of two proteins (Protein A, MW 64,000; Protein B, MW 46,000).
- Cyclic AMP inhibited the phosphorylation of one protein (Protein C, MW 18,000).
- Phosphorylation reached maximal levels within 5 minutes, with half-maximal effects at approximately 1.0 x 10(-7) M cAMP. Cyclic GMP and cyclic IMP showed minimal effects.
Conclusions:
- Cyclic AMP plays a significant role in regulating protein phosphorylation in Coprinus macrorhizus.
- Specific proteins (A, B, and C) are direct or indirect targets of cAMP-mediated signaling.
- The findings provide insights into the molecular mechanisms governing fungal growth and development.