Protein kinase CK2 phosphorylates the Fas‐associated factor FAF1 in vivo and influences its transport into the nucleus

FEBS Letters

Jessen, Vibeke¹  Olsen, Birgitte B.¹  Boldyreff, Brigitte¹  Højrup, Peter¹  Issinger, Olaf-Georg¹ 

[1] Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark

关键词: Fas-associated factor;    FAF1;    protein kinase CK2;    Phosphorylation;    Apoptosis;    Nuclear translocation;   

DOI  :  10.1016/S0014-5793(03)00575-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously identified the Fas-associated factor FAF1 as an in vitro substrate of protein kinase CK2 and determined Ser289 and Ser291 as phosphorylation sites. Here we demonstrate that these two serine residues are the only sites phosphorylated by CK2 in vitro, and that at least one site is phosphorylated in vivo. Furthermore, we analyzed putative physiological functions of FAF1 phosphorylation. The ability of FAF1 to potentiate Fas-induced apoptosis is not influenced by the FAF1 phosphorylation status; however, the nuclear import of a phosphorylation-deficient FAF1 mutant was delayed in comparison to wild-type FAF1.

【 授权许可】

Unknown