Delbridge, L.M.; Koutsifeli, P.; Fong, S.P.; Annandale, M.; Weeks, K.L.; Bell, J.R.; Mellor, K.M. Glycophagy – the Physiological Perspective on A Newly Characterized Glycogen-Selective Autophagy. Preprints2022, 2022080142. https://doi.org/10.20944/preprints202208.0142.v1
Delbridge, L.M., Koutsifeli, P., Fong, S.P., Annandale, M., Weeks, K.L., Bell, J.R., & Mellor, K.M. (2022). Glycophagy – the Physiological Perspective on A Newly Characterized Glycogen-Selective Autophagy. Preprints. https://doi.org/10.20944/preprints202208.0142.v1
Delbridge, L.M., James R. Bell and Kimberley M. Mellor. 2022 "Glycophagy – the Physiological Perspective on A Newly Characterized Glycogen-Selective Autophagy" Preprints. https://doi.org/10.20944/preprints202208.0142.v1
Degradation of intracellular components through autophagy is a fundamental process to maintain cellular integrity and homeostasis. Recently a glycogen-selective autophagy pathway has been described, termed ‘glycophagy’. Glycogen is a primary storage depot and regulator of glucose availability, and glycophagy is emerging as a critical physiological process involved in energy metabolism. Glycophagy-mediated degradation of glycogen appears to operate in parallel with the well-described canonical pathway of glycogenolysis involving glycogen phosphorylase. Evidence suggests that starch-binding domain protein-1 (Stbd1) is a key glycogen-binding protein involved in tagging glycogen for glycophagy, and that Gabarapl1 is primarily involved as the Atg8 family protein recruiting the Stbd1-glycogen complex into the forming glycophagosome. The nuances of glycophagy protein machinery, regulation and lysosomal glucose release are yet to be fully elucidated. In this mini-review, we critically analyze the current evidence base for glycophagy as a selective-autophagy process of physiological importance and highlight areas where further investigation is warranted.
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