Journal article
The recruitment of AMP-activated protein kinase to glycogen is regulated by autophosphorylation
Y Oligschlaeger, M Miglianico, D Chanda, R Scholz, RF Thali, R Tuerk, DI Stapleton, PR Gooley, D Neumann
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2015
Abstract
Background: AMP-activated protein kinase (AMPK) is a current drug target. AMPK can attach to glycogen granules. Results: Autophosphorylation of AMPK prevents its association with glycogen. Conclusion: Subcellular localization of AMPK is affected by the kinase autophosphorylation status. Significance: Understanding the regulation of AMPK at subcellular level is crucial for the currently pursued drug targeting approach.
Grants
Awarded by Schweizerische Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Funding Acknowledgements
Research in the laboratory of D. N. was supported by the Netherlands Organization for Scientific Research (NWO) (VIDI Grant 864.10.007). This work was also supported by Swiss National Science Foundation Grant 3100A-0114137, EU FP6 Contract LSHM-CT-2004-005272 (EXGENESIS), and Graduate Training Fellowships ETHIIRA 36/05-3 and 32/05-3 (for R. S. and R. F. T.).Recipient of a Marie Curie fellowship (Grant PIIF-GA-2012-332230).