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Klemm, J. D., Schreiber, S. L. & Crabtree, G. R. Dimerization as a regulatory mechanism in signal transduction.
Phosphorylation by protein kinases is the most common and important regulatory mechanism in signal transduction.
It is highly relevant, therefore, to take into account the possible effect of such mechanism in signal detection in noisy environments.
In conclusion, we have shown that elongation of the NKG2D ligand MICA abrogates NKG2D signaling, consistent with a role for the kinetic-segregation mechanism in signal transduction through NK receptors.
Protein phosphorylation is a central regulatory mechanism in signal transduction involved in most biological processes.
In Klemm [ 5] the role of dimerisation as a regulatory mechanism in signal transduction is analysed and discussed.
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However, Est-6 involvement in signal dynamics does not preclude a role of additional mechanisms in signal termination.
Phosphorylation by protein kinases is one of the most common and important regulatory mechanisms in signal transduction among all organisms [ 29].
Reversible protein cysteine nitrosylation (S-nitrosylation) is a common mechanism utilized in signal transduction and other diverse cellular processes.
Hence, this review emphasizes on the structure of BMP and its receptors, and its role in integrated regulatory mechanisms in signaling.
The purpose of this work is to suggest coupled approaches where molecular mechanisms in signalling pathways will be characterised simultaneously with the corresponding mesoscopic measurements.
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