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.

Links

Publisher Full Text

Authors

Langer S, Okar DA, Schultz J, Lenzen S, Baltrusch S

Institution

Institute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.

Source

FEBS letters 586:10 2012 May 21 pg 1419-25

MeSH

Animals
Blotting, Western
COS Cells
Cercopithecus aethiops
Cyclic AMP
Dimerization
Fluorescence Resonance Energy Transfer
Forskolin
Liver
Phosphofructokinase-2
Phosphorylation
Rats
Serine
Two-Hybrid System Techniques

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22668829