Does AMPK bind glycogen in skeletal muscle or is the relationship correlative?
Autor: | Frankish BP; Sport, Exercise and Nutrition Sciences, School of Allied Health, Human Services and Sport, La Trobe University, Melbourne, VIC 3086, Australia., Murphy RM; Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, School of Agriculture, Biomedicine and Environment, La Trobe University, Melbourne, VIC 3086, Australia Insert Affiliation Text Here. |
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Jazyk: | angličtina |
Zdroj: | Essays in biochemistry [Essays Biochem] 2024 Nov 18; Vol. 68 (3), pp. 337-347. |
DOI: | 10.1042/EBC20240006 |
Abstrakt: | Since its discovery over five decades ago, an emphasis on better understanding the structure and functional role of AMPK has been prevalent. In that time, the role of AMPK as a heterotrimeric enzyme that senses the energy state of various cell types has been established. Skeletal muscle is a dynamic, plastic tissue that adapts to both functional and metabolic demands of the human body, such as muscle contraction or exercise. With a deliberate focus on AMPK in skeletal muscle, this review places a physiological lens to the association of AMPK and glycogen that has been established biochemically. It discusses that, to date, no in vivo association of AMPK with glycogen has been shown and this is not altered with interventions, either by physiological or biochemical utilisation of glycogen in skeletal muscle. The reason for this is likely due to the persistent phosphorylation of Thr148 in the β-subunit of AMPK which prevents AMPK from binding to carbohydrate domains. This review presents the correlative data that suggests AMPK senses glycogen utilisation through a direct interaction with glycogen, the biochemical data showing that AMPK can bind carbohydrate in vitro, and highlights that in a physiological setting of rodent skeletal muscle, AMPK does not directly bind to glycogen. (© 2024 The Author(s).) |
Databáze: | MEDLINE |
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