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

Birgitte B Olsen, Vibeke Jessen, Peter Højrup, Olaf-Georg Issinger, Brigitte Boldyreff

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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.
Original languageEnglish
JournalFEBS Letters
Volume546
Issue number2-3
Pages (from-to)218-22
Number of pages4
ISSN0014-5793
DOIs
Publication statusPublished - 10. Jul 2003

Keywords

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Carrier Proteins
  • Casein Kinase II
  • Cell Nucleus
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Protein-Serine-Threonine Kinases
  • Serine
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

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