In:
FEBS Letters, Wiley, Vol. 550, No. 1-3 ( 2003-08-28), p. 23-29
Abstract:
6‐Phosphofructo‐2‐kinase catalyzes the synthesis and degradation of fructose 2,6‐bisphosphate, activator of phosphofructokinase‐1 and inhibitor of fructose 1,6‐bisphosphatase. These properties confer to this bifunctional enzyme a key role in the control of glycolysis and gluconeogenesis. Several mammalian isozymes generated by alternative splicing from four genes, designated pfkfb1–4, have been identified. The results presented in this study demonstrate the expression of the pfkfb3 gene in C2C12 cells and its downregulation during myogenic cell differentiation. We also show that the decrease of ubiquitous 6‐phosphofructo‐2‐kinase isozyme levels, product of pfkfb3 gene, is due to its enhanced degradation through the ubiquitin‐proteasome proteolytic pathway.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/S0014-5793(03)00808-1
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
1460391-3
SSG:
12
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