This mode of regulation had been suggested for only a few metabolic enzymes, however,  it was not clear why decreasing the sensitivity of a response to a signal was important. 

In the work published in Communication Biology https://rdcu.be/em0vB, a thermodynamic analysis of the linkage between heterotropic ligand binding to Diaphanous , a Diaphanous Related Formin (DRF) is presented.  The analysis enabled us to propose a model that utilizes negative cooperativity as a key element in regulating Diaphanous 1 activity that can also be extended to include all DRFs. By exploiting negative cooperativity, DRFs maintain a reserve of inactivated DIAPH1 for other cellular processes.  And unlike the sharp, switch-like functional transitions that accompany small changes in ligand concentration in allosteric systems that make use of positive cooperative binding, negative binding cooperativity in DRFs enables more gradual responses to cellular processes that require prolonged and sustained regulation, such as cell migration, phagocytosis, and cytokinases.