Journal article
AMPK β subunits display isoform specific affinities for carbohydrates
A Koay, B Woodcroft, EJ Petrie, H Yue, S Emanuelle, M Bieri, MF Bailey, M Hargreaves, JT Park, KH Park, S Ralph, D Neumann, D Stapleton, PR Gooley
FEBS Letters | WILEY | Published : 2010
Abstract
AMP-activated protein kinase (AMPK) is a heterotrimer of catalytic (α) and regulatory (β and γ) subunits with at least two isoforms for each subunit. AMPK β1 is widely expressed whilst AMPK β2 is highly expressed in muscle and both β isoforms contain a mid-molecule carbohydrate-binding module (β-CBM). Here we show that β2-CBM has evolved to contain a Thr insertion and increased affinity for glycogen mimetics with a preference for oligosaccharides containing a single α-1,6 branched residue. Deletion of Thr-101 reduces affinity for single α-1,6 branched oligosaccharides by 3-fold, while insertion of this residue into the equivalent position in the β1-CBM sequence increases affinity by 3-fold, ..
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Awarded by Australian Research Council
Funding Acknowledgements
We thank Prof. Michael Parker and Dr. John Scott for critical reading of the manuscript. This work was supported by Australian Research Council and Rowden White Foundation for project and equipment funding for P.R.G., the National Health and Medical Research Council for D.S., by the European Union FP6 contract LSHM-CT-2004-005272 (EXGENESIS). A.K. is a recipient of a Melbourne University International Research Scholarship; S.E. a recipient of a Sir John and Lady Higgins Research Scholarship; and M.B. a recipient of a Swiss National Science Foundation fellowship.