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

FEBS Letters

Duran, Joan¹  Riera, Lluı́s¹  Viñals, Francesc¹  Perales, Jose C¹  Obach, Mercè¹  Navarro-Sabaté, Aurea¹  Bartrons, Ramon¹  Ventura, Francesc¹  Rosa, Jose Luis¹ 

[1] Unitat de Bioquı́mica i Biologia Molecular, Departament de Ciències Fisiològiques II, Campus de Bellvitge, Universitat de Barcelona, Feixa Llarga s/n, Pavelló de Govern, 4 planta E-08907 L'Hospitalet, Spain

关键词: 6-phosphofructo-2-kinase/fructose 2;    6-bisphosphatase;    Glycolysis;    Ubiquitin;    Proteasome;    Myogenic differentiation;    PFK-2;    6-phosphofructo-2-kinase [EC 2.7.1.105]/fructose 2;    6-bisphosphatase [EC 3.1.3.46];    uPFK-2;    ubiquitous 6-phosphofructo-2-kinase/fructose 2;    6-bisphosphatase;    Fru-2;    6-P2;    fructose 2;    6-bisphosphate;    LLnL;    N-acetyl-leucinyl-leucinyl-N-norleucinal;   

DOI  :  10.1016/S0014-5793(03)00808-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown