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. Author manuscript; available in PMC: 2024 Apr 1.
Published in final edited form as: Curr Opin Struct Biol. 2023 Jan 27;79:102530. doi: 10.1016/j.sbi.2023.102530

Figure 4. Filaments exploit many regulation modalities.

Figure 4.

A. A spike in substrate concentration shifts protomers into filaments, inactivating the enzyme and preventing an overconsumption of substrate and cellular toxicity (glucokinase 1). B. Filaments stabilize the active form of the enzyme (CTP synthase 1). C. Filaments act as a cooperative switch, flipping the entire filament into the active or inactive conformation upon local binding of the activator or inhibitor, respectively (CTP synthase 2). D. Filaments stabilize the allosteric site of a protein, supporting the active or inactive conformations of the enzyme (PRPP synthetase 1). E. In the presence of high feedback inhibitor, filaments mitigate inhibition, allowing for sustained enzyme activity (IMP dehydrogenase). F. Filament assembly facilitates substrate channeling between the active sites in different domains within the enzyme (aldehyde-alcohol dehydrogenase). G. List of filament-forming proteins used as examples in this manuscript.