Premium
Protein kinase CK2 phosphorylates the Fas‐associated factor FAF1 in vivo and influences its transport into the nucleus
Author(s) -
Olsen Birgitte B.,
Jessen Vibeke,
Højrup Peter,
Issinger Olaf-Georg,
Boldyreff Brigitte
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00575-1
Subject(s) - phosphorylation , phosphorylation cascade , serine , microbiology and biotechnology , protein phosphorylation , protein kinase a , kinase , biology , chemistry
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.