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Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
586
Issue
10
Identifiers
DOI: 10.1016/j.febslet.2012.03.066
Keywords
  • 6-Phosphofructo-2-Kinase/Fructose-2
  • 6-Bisphosphatase
  • Ser-32 Phosphorylation
  • Dimerization
  • Bifunctional Enzyme
  • Mammalian Two-Hybrid System
  • Fluorescence Resonance Energy Transfer
Disciplines
  • Biology

Abstract

Abstract The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2) is a key regulator of carbohydrate metabolism in liver. The goal of this study was to elucidate the regulatory role of Ser-32 phosphorylation on the kinase domain mediated dimerization of PFK-2/FBPase-2. Fluorescence-based mammalian two-hybrid and sensitized emission fluorescence resonance energy transfer analyses in cells revealed preferential binding within homodimers in contrast to heterodimers. Using isolated proteins a close proximity of two PFK-2/FBPase-2 monomers was only detectable in the phosphorylated enzyme dimer. Thus, a flexible kinase interaction mode exists, suggesting dimer conformation mediated coupling of hormonal and posttranslational enzyme regulation to the metabolic response in liver. Structured summary of protein interactions PFK-2/FBPase-2physically interacts with PFK-2/FBPase-2 by fluorescent resonance energy transfer (View Interaction: 1, 2) PFK-2/FBPase-2physically interacts with PFK-2/FBPase-2 by two hybrid (View interaction)

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