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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Riera L,Obach M,Navarro-Sabaté A,Duran J,Perales JC,Viñals F,Rosa JL,Ventura F,Bartrons Rdoi
10.1016/s0014-5793(03)00808-1keywords:
subject
Has Abstractpub_date
2003-08-28 00:00:00pages
23-9issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579303008081journal_volume
550pub_type
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