Article
Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesis.
The Biochemical journal - 15 Feb 2006
Cao Heping, Deterding Leesa J, Venable John D, Kennington Elizabeth A, Yates John R, Tomer Kenneth B, Blackshear Perry J
Abstract excerpt
Tristetraprolin (TTP) is a zinc-finger protein that binds to AREs (AU-rich elements) within certain mRNAs and causes destabilization of those mRNAs. Mice deficient in TTP develop a profound inflammatory syndrome with erosive arthritis, autoimmunity and myeloid hyperplasia. Previous studies showed that TTP is phosphorylated extensively in intact cells. However, limited information is available about the identities...
Topics
- Amino Acid Sequence
- Anti-Inflammatory Agents
- Binding Sites
- Cell Line
- Humans
- Mass Spectrometry
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Phosphorylation