Activation of cytoplasmic trehalase by cyclic-AMP-dependent and cyclic-AMP-independent signalling pathways in the yeast Candida utilis

Article Abstract:

A study of signaling pathways involved in the induction of cytoplasmic trehalase in Candida utilis reveals the participation of three different mechanisms that respond to diverse environmental or nutritional conditions to enhance trehalase activity. The cAMP-independent pathway is activated by protein synthesis and glucose and is functional only in repressed cells, while the glucose-stimulated pathway stimulates the target enzymes through some glucose-repressive element expression. A temporary cAMP enhancement and protein kinase activation are essential for the transduction of this signal.

Physiological aspects, Cellular signal transduction, Cytoplasm

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Glucose-induced, cyclic-AMP-independent signalling pathway for activation of neutral trehalase in the fission yeast Schizosaccharomyces pombe

Article Abstract:

A cyclic-adenylic acid (cAMP) signal and cytoplasmic neutral trehalase activation in derepressed growing cells of Schizosaccharomyces pombe is observed by adding glucose. The trehalase activation requires a cAMP-dependent protein kinase (PKA1). During the presence of a cAMP-independent protein kinase, the activation occurs via a glucose- induced phosphorylation mechanism. Trehalase is the natural substrate for PKA1 and is a target for at least another protein kinase of the fission yeast.

Enzymes

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Protein kinase Sck1 is involved in trehalase activation by glucose and nitrogen source in the fission yeast Schizosaccharomyces pombe

Article Abstract:

Disruptant strains of Schizosaccharomyces pombe that lack either Sck1, Pka1 or both protein kinases were used to assess the potential of trehalase as a common target for Sck1 and Pka1. Except in repressed cells, Sck1 was found involved in activation of trehalase. It was also found essential in the mechanism which is responsible for trehalase stimulation triggered by glucose and nitrogen source.

Protein kinases

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