The role of protein translocation in the regulation of glycogen metabolism

• Published in: Journal of cellular biochemistry 2008-05, Vol.104 (2), p.435-443
• Main Authors: Jurczak, Michael J., Danos, Arpad M., Rehrmann, Victoria R., Brady, Matthew J.
• Format: Article
• Language: English
• Subjects: Animals; glucokinase; Glucose - metabolism; GLUT4; Glycogen - metabolism; glycogen synthase; hexokinase; Humans; insulin; Liver - metabolism; Muscle, Skeletal - metabolism; phosphorylase; Protein Transport - physiology
• ISSN: 0730-2312; 1097-4644
• DOI: 10.1002/jcb.21634

Early biochemical analyses of metabolic pathways assumed that the free diffusion of substrates and enzymes in an evenly mixed cellular space provided the interactions that enabled reactions to proceed. Metabolic complexes have since been shown to assemble and disassemble in response to changes in cellular conditions, and in turn, to channel metabolic intermediates within discreet cellular compartments, allowing for the efficient use or storage of energy. A fundamental component to the formation of metabolic complexes and the channeling of metabolites is the translocation of enzymes in response to specific extra‐ and intracellular signals. These generalities play an important role in the metabolism of glucose to glycogen within skeletal muscle and liver. In this review, the similarities and differences in skeletal muscle and liver glucose metabolism with regards to glucose transport and intracellular processing will be addressed during the fasted to fed transition. More specifically, the importance of isoform expression and protein translocation in the tissue specific control of glucose homeostasis will be covered. J. Cell. Biochem. 104: 435–443, 2008. © 2007 Wiley‐Liss, Inc.