Regulation of ubiquitous 6-phosphofructo-2-kinase by the ubiquitin-proteasome proteolytic pathway during myogenic C2C12 cell differentiation.

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 Lett

journal_title

FEBS letters

authors

Riera L,Obach M,Navarro-Sabaté A,Duran J,Perales JC,Viñals F,Rosa JL,Ventura F,Bartrons R

doi

10.1016/s0014-5793(03)00808-1

keywords:

subject

Has Abstract

pub_date

2003-08-28 00:00:00

pages

23-9

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579303008081

journal_volume

550

pub_type

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