Journal
ACTA PHYSIOLOGICA
Volume 199, Issue 4, Pages 489-498Publisher
WILEY
DOI: 10.1111/j.1748-1716.2010.02131.x
Keywords
carbohydrate; glycogen synthase; glycogenin; laforin; malin; protein translocation
Categories
Funding
- NSERC of Canada
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Despite decades of studying muscle glycogen in many metabolic situations, surprisingly little is known regarding its regulation. Glycogen is a dynamic and vital metabolic fuel that has very limited energetic capacity. Thus its regulation is highly complex and multifaceted. The stores in muscle are not homogeneous and there appear to be various metabolic pools. Each granule is capable of independent regulation and fundamental aspects of the regulation appear to be associated with a complex set of proteins (some are enzymes and others serve scaffolding roles) that associate both with the granule and with each other in a dynamic fashion. The regulation includes altered phosphorylation status and often translocation as well. The understanding of the roles and the regulation of glycogenin, protein phosphatase 1, glycogen targeting proteins, laforin and malin are in their infancy. These various processes appear to be the mechanisms that give the glycogen granule precise, yet dynamic regulation.
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