Mor, I., Cheung, E.C. and Vousden, K.H. (2011) Control of glycolysis through regulation of PFK1: old friends and recent additions. Cold Spring Harbor Symposia on Quantitative Biology, 2011(76), pp. 211-216. (doi: 10.1101/sqb.2011.76.010868)
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Publisher's URL: http://dx.doi.org/10.1101/sqb.2011.76.010868
Abstract
Regulation of glucose metabolism is a crucial aspect of cell physiology in normal and disease conditions. Many regulatory events are involved in determining the metabolic fate of glucose and the pathways into which it is directed. The first reaction that commits glucose to the glycolytic pathway is catalyzed by the enzyme phosphofructokinase-1 (PFK-1) and is tightly regulated. One of the most potent activators of PFK-1 is fructose 2,6 bisphosphate (F2,6BP) and its cellular levels are correlated with glycolytic flux. F2,6BP is synthesized and degraded by a family of bifunctional enzymes—the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatases (PFKFB). The interplay among F2,6BP levels, the enzymes that generate and degrade it, and PFK-1 activity has important consequences for several different aspects of cell metabolism as well as for systemic metabolic conditions. TIGAR, a recently identified F2,6 bisphosphatase (F2,6BPase), could also contribute to this complexity and participate in shaping the metabolic profile of the cell.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Vousden, Karen |
Authors: | Mor, I., Cheung, E.C., and Vousden, K.H. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
Journal Name: | Cold Spring Harbor Symposia on Quantitative Biology |
Publisher: | Cold Spring Harbor Laboratory |
ISSN: | 0091-7451 |
ISSN (Online): | 1943-4456 |
Published Online: | 17 November 2011 |
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