The regulation of muscle glycogen: the granule and its proteins
Abstract
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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Upregulation of key metabolic genes initiated by release of glycogen-bound proteins may explain how glycogen depletion affects insulin-dependent muscle glucose uptake.
“The upregulation of key metabolic genes initiated by the release of glycogen-bound proteins may, at least in part, explain how glycogen depletion affects insulin-dependent muscle glucose uptake (Steinberg et al. 2006;Graham et al. 2010).”
From Towards the minimal amount of exercise for improving metabolic health: beneficial effects of reduced-exertion high-intensity interval training (2012) · cites this paper as Graham et al. 2010
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- Authors
- Graham, T. E., Yuan, Z., Hill, A. K., & Wilson, R. J.
- Affiliations
- University of Guelph (CA)
- Corresponding author
- Graham, T. E.
- ORCID
- Hill, A. K.
- Venue
- Acta Physiologica
- Publisher
- Wiley
- Published
- 2010-07
- Volume
- 199
- Issue
- 4
- Pages
- 489-498
- ISSN
- 1748-1708 (ISSN-L)
- 1748-1716
- OpenAlex
- W1923002492
- Cited by
- 69
- References
- 62
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 5 · 2017: 4 · 2016: 4 · 2015: 10 · 2014: 4 · 2013: 7 · 2012: 13
- FWCI
- 1.19
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Acta Physiologica (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Rheumatology › Glycogen Storage Diseases and Myoclonus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- muscle glycogen, glycogen granules, glycogenin, protein phosphatase 1, laforin, malin, protein phosphorylation, protein translocation, glycogen metabolism
- MeSH terms
- Animals, Carrier Proteins, Cytoplasmic Granules, Glucosyltransferases, Glycogen, Glycogen Synthase, Glycoproteins, Humans, Phosphorylation, Muscle, Skeletal, Ubiquitin-Protein Ligases, Protein Tyrosine Phosphatases, Non-Receptor, Protein Phosphatase 1, AMP-Activated Protein Kinases
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