PHAS‐I phosphorylation in response to foetal bovine serum (FBS) is regulated by an ERK1/ERK2‐independent and rapamycin‐sensitive pathway in 3T3‐L1 adipocytes

FEBS Letters

Atkinson, Peter G.P.¹  Arnott, Caroline H.¹  Sale, Elizabeth M.¹  Sale, Graham J.¹ 

[1] Department of Biochemistry, School of Biological Sciences, Biomedical Sciences Building, Bassett Crescent East, Southampton SO16 7PX, UK

关键词: PHAS-I;    Fetal bovine serum;    ERK1/ERK2;    p70S6k;    Antisense oligonucleotide;    Rapamycin;    FBS;    foetal bovine serum;    ERK1/ERK2;    extracellular signal regulated kinases 1 and 2 (also known as p44 and p42 MAP kinase);    MEK;    MAP kinase kinase/ERK kinase;    eIF;    eukaryotic initiation factor;    ODN;    oligonucleotide;    PHAS-I;    phosphorylated heat- and acid-stable protein regulated by insulin;    PI3K;    phosphatidylinositol 3-kinase;   

DOI  :  10.1016/S0014-5793(97)00266-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The phosphorylation state of PHAS-I is thought to be important in the regulation of protein synthesis initiation. PHAS-I phosphorylation significantly increases in response to growth factors and insulin. ERK1/ERK2 have previously been implicated as PHAS-I kinases. Present work utilised a specific phosphorothioate oligonucleotide antisense strategy against ERK1/ERK2 to determine whether ERK1/ERK2 mediate FBS-stimulated PHAS-I phosphorylation in vivo. Depleting >90% of cellular ERK1/ERK2 had no effect on FBS-stimulated PHAS-I phosphorylation. However, treatment of cells with a specific p70^S6k pathway inhibitor, rapamycin, markedly attenuated FBS-stimulated PHAS-I phosphorylation. These results indicate that PHAS-I phosphorylation in response to FBS occurs through an ERK1/ERK2-independent and rapamycin-sensitive pathway in 3T3-L1 adipocytes.

【 授权许可】

Unknown