Cada grup assignat ha de respondre la seva pregunta

Team

In analyzing how a cell responds to stress, you discover several induced phosphorylation events on a membrane-associated protein, X. 1
Phosphorylation of protein X on Thr122 induces its interaction with protein Y. Describe possible alternative mechanisms by which this
modification might induce binding to protein Y. Propose experiments to distinguish between these possibilities.
Phosphorylation of the protein X from Question 1 on Ser54 disrupts its interaction with protein Z. Describe possible mechanisms by which this 2
modification might disrupt binding to protein Z.
Sometimes, phosphorylation of a protein on a specific residue leads to the degradation of that protein. Describe the general mechanisms by 3
which degradation can be mediated by phosphorylation, and the intervening steps between phosphorylation and degradation.
One mechanism used by phosphorylation is priming, where one kinase phosphorylates the target, creating a binding site for a second kinase. 4
Recruitment of the second kinase subsequently leads to phosphorylation on a second (or additional) site. What kinds of kinetic responses might
result from a protein that is controlled by a priming mechanism? Describe additional features of the signaling system that would be necessary in
your model.
Efforts are underway to map the full complement of protein post-translational modifications in various cells under different conditions. Is it 5
realistic to expect that such a task will ever be completed? What are the major challenges in such an effort?
Is has been suggested that some experimentally detected post-translational modifications of specific sites might have no function, or may even 6
be detrimental to the cell. Under what conditions might this be the case?
A number of enzymes that modify proteins contain a reader domain that binds to the modified substrate. For example, nonreceptor tyro-sine 7
kinases have SH2 domains that bind to tyrosine-phosphorylated peptides; and histone acetyl transferases have bromo domains that bind
acetylated lysines. What effect will these reader domains have on modification by such enzymes, and under what conditions would such an
arrangement be useful?

How might you engineer a system, based on a ubiquitin E3 ligase, to degrade a particular protein of choice in the cell? 8