A scientist is studying a signal transduction pathway that is controlled by a re

Question

A scientist is studying a signal transduction pathway that is controlled by a receptor tyrosine kinase and has identified a MAP kinase that functions as part of the signaling cascade. She engineers an altered form of the MAP kinase in which residues that are phosphorylated when the signaling pathway is turned on are replaced with amino acids that cannot be phosphorylated. What affect would this have on the signaling pathway? The scientist has also identified a GTP-ase that is involved in an interaction with the receptor after it dimerizes. What would be the effect on signaling of adding GTPgS to tissue culture cells expressing the mutated version of the MAP kinase? (Note - GTPgS can bind to GTPases but cannot be converted to GDP). Explain your answers.

Explanation / Answer

Phosphorylation and De phosphorylation are two main Pathways by which many parties are controlled that is either they are turned on or turned off. Phosphorylation of amino acids in map kinase give sir signal for the signal cascade mechanism downside. If these amino acids are replaced by the ones which Can't phosphorylated, the signalling pathway would be stopped.

If GTPgS bind and doesn't hydrolyse, it wouldn't be converted to GDP and hence the signalling would be stopped by permanently engaging the recepies. Until hydrolysis is not occuring the receptors can not bind to new signal.

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