Hi there,
I am starting to work with a new kinase in our lab and we are facing up with a concerning fact in our preliminary data. Our experiments reveal (performed under the same condition as well as cell line) that this kinase seems to stabilize and degrade a specific potential substrate. We are considering the existence of a potential negative feedback loop, however, we would like to know if anyone with more experience than us might have more ideas.
Kind regards,
Alex
What is the target? If phosphorylation of the substrate is a target for ubiquitination it can degrade.
I agree with the above answer.
It is possible that phosphorylation of a protein allows more enzymes to work on it any add other marks (eg. Hydroxylation) which makes it vulnerable for degradation by facilitating its interaction with ubiquitin ligase enaymes.
You may check the following paper for further explanation.
Article α-Ketoglutarate Inhibits Thrombosis and Inflammation by Prol...
It needs to be coupled to in vivo monitoring. Kinetics is useful in affinity binding, but factors in vivo might have different effects because of the presence of allosteric modifiers like NO, Citruulin, methylation etc. That is what led to the present dogmas of glycolysis and Meyerhof revised his earlier concepts on ALDOA, TPI and pyruvate kinase (PK). Warburg never did that. Present confusion emanates from two dogmas on ALDOA and PK.
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