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- W2150084081 abstract "Muscle fructose-1,6-bisphosphatase (FBP2), a regulatory enzyme of glyconeogenesis, binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis. Here, we show that the quaternary structure of FBP2 plays a crucial role in this interaction, and that the AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Moreover, we demonstrate that truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions. This strengthens the recently raised hypothesis that FBP2 evolved as a regulator not only for glycogen storage but also for mitochondrial function in contracting muscle." @default.
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- W2150084081 date "2014-03-01" @default.
- W2150084081 modified "2023-09-27" @default.
- W2150084081 title "Changes in quaternary structure of muscle fructose-1,6-bisphosphatase regulate affinity of the enzyme to mitochondria" @default.
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- W2150084081 doi "https://doi.org/10.1016/j.biocel.2013.12.015" @default.
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