Interaction of tetrameric and dimeric FBP2 with CAMK2α, HIF1α and ALDOA

Abstract

Macromolecular interactions are common mechanisms of protein function regulation. Emerging role of muscle fructose 1,6-bisphospatase (FBP2) in memory formation and cancer cells survival was hypothesized to be regulated by such interactions. FBP2 exists as mixture of different oligomeric states which presumably may interact with their binding partners in a different mode. Results presented here show how alterations of FBP2 quaternary structure affects interactions with such proteins as CAMK2?, HIF1? or ALDOA. We show that a dimeric FBP2 is preferred form of the enzyme for interaction with CAMK2?. On the other hand, an inactive tetrameric T-state of FBP2 binds HIF1? and, to a lesser extent, ALDOA stronger than the dimeric and an active R-state tetrameric FBP2.