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More on target with protein phosphorylation: conferring specificity by location.

Maree C. Faux, John D. Scott

Open publisher page 225 citations

Abstract

One important regulatory mechanism in the control of phosphorylation events is the subcellular location of phosphatases of kinases. Several serine/threonine phosphatases and kinases have now been shown to be associated with targeting subunits; these contribute to the organization and specificity of signal transduction pathways by favoring the accessibility of their enzymes to certain substrates.

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What this paper is about

One important regulatory mechanism in the control of phosphorylation events is the subcellular location of phosphatases of kinases. Several serine/threonine phosphatases and kinases have now been shown to be associated with targeting subunits; these contribute to the organization and specificity of signal transduction pathways by favoring the accessibility of their enzymes to certain substrates.

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Available abstract

One important regulatory mechanism in the control of phosphorylation events is the subcellular location of phosphatases of kinases. Several serine/threonine phosphatases and kinases have now been shown to be associated with targeting subunits; these contribute to the organization and specificity of signal transduction pathways by favoring the accessibility of their enzymes to certain substrates.

Key concepts: Phosphorylation, Kinase, Serine, Phosphatase, Threonine, Protein phosphorylation, Signal transduction, Protein-Serine-Threonine Kinases

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