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

被引：30

作者：

Riera, L ^{[1
]}

Obach, M ^{[1
]}

Navarro-Sabaté, A ^{[1
]}

Duran, J ^{[1
]}

Perales, JC ^{[1
]}

Viñals, F ^{[1
]}

Rosa, JL ^{[1
]}

Ventura, F ^{[1
]}

Bartrons, R ^{[1
]}

机构：

[1] Univ Barcelona, Dept Ciencias Fisiol 2, Unitat Bioquim & Biol Mol, E-08907 Lhospitalet De Llobregat, Spain

来源：

FEBS LETTERS | 2003年 / 550卷 / 1-3期

关键词：

6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase; glycolysis; ubiquitin; proteasome; myogenic differentiation;

D O I：

10.1016/S0014-5793(03)00808-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：23 / 29

页数：7

共 39 条

[1] Degradation of myogenic transcription factor MyoD by the ubiquitin pathway in vivo and in vitro: Regulation by specific DNA binding [J].