Abstract
The AMP-activated protein kinase (AMPK) is a heterotrimeric complex with central roles in cellular energy sensing and the regulation of metabolism and exercise adaptations. AMPK regulatory β subunits contain a conserved carbohydrate-binding module (CBM) that binds glycogen, the major tissue storage form of glucose. Research over the past two decades has revealed that the regulation of AMPK is impacted by glycogen availability, and glycogen storage dynamics are concurrently regulated by AMPK activity. This growing body of research has uncovered new evidence of physical and functional interactive roles for AMPK and glycogen ranging from cellular energy sensing to the regulation of whole-body metabolism and exercise-induced adaptations. In this review, we discuss recent advancements in the understanding of molecular, cellular, and physiological processes impacted by AMPK-glycogen interactions. In addition, we appraise how novel research technologies and experimental models will continue to expand the repertoire of biological processes known to be regulated by AMPK and glycogen. These multidisciplinary research advances will aid the discovery of novel pathways and regulatory mechanisms that are central to the AMPK signaling network, beneficial effects of exercise and maintenance of metabolic homeostasis in health and disease.
Highlights
The AMP-activated protein kinase (AMPK) is a heterotrimer composed of a catalytic α subunit and regulatory β and γ subunits, which becomes activated in response to a decrease in cellular energy status
This physical interaction is mediated by the carbohydrate-binding module (CBM) located within the AMPK β subunit and is thought to allow AMPK to function as a sensor of stored cellular energy
While glycogen is stored in multiple tissues throughout the body, this review will primarily focus on the physical interactions underlying the AMPK β subunit binding to glycogen and its potential functional links to glycogen storage dynamics in the liver and skeletal muscles, as these tissues are central to metabolic and exercise-regulated biological processes
Summary
The AMP-activated protein kinase (AMPK) is a heterotrimer composed of a catalytic α subunit and regulatory β and γ subunits, which becomes activated in response to a decrease in cellular energy status. A significant body of evidence demonstrates that AMPK binds glycogen This physical interaction is mediated by the carbohydrate-binding module (CBM) located within the AMPK β subunit and is thought to allow AMPK to function as a sensor of stored cellular energy. While glycogen is stored in multiple tissues throughout the body, this review will primarily focus on the physical interactions underlying the AMPK β subunit binding to glycogen and its potential functional links to glycogen storage dynamics in the liver and skeletal muscles, as these tissues are central to metabolic and exercise-regulated biological processes. Following a brief background on the regulation of AMPK and glycogen, this review will critically assess the recent advances and focus primarily on studies within the past two decades that have added to our understanding of the physical basis of AMPK-glycogen binding and its potential functional interactions in exercise and metabolism. Key remaining biological questions related to the interactive roles of AMPK and glycogen will be posed along with a discussion of research advancements that are feasible in the decade with new technologies and experimental models to determine how AMPK-glycogen binding may be therapeutically targeted in health and disease
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
