| First Author | Devries IL | Year | 2010 |
| Journal | FEBS Lett | Volume | 584 |
| Issue | 23 | Pages | 4725-30 |
| PubMed ID | 21056038 | Mgi Jnum | J:200508 |
| Mgi Id | MGI:5508737 | Doi | 10.1016/j.febslet.2010.10.060 |
| Citation | Devries IL, et al. (2010) Consequences of IkappaB alpha hydroxylation by the factor inhibiting HIF (FIH). FEBS Lett 584(23):4725-30 |
| abstractText | The factor inhibiting HIF-1 (FIH-1) hydroxylates many ankyrin repeat-containing proteins including IkappaBalpha. It is widely speculated that hydroxylation of IkappaBalpha has functional consequences, but the effects of hydroxylation have not been demonstrated. We prepared hydroxylated IkappaBalpha and compared it to the unhydroxylated protein. Urea denaturation and amide H/D exchange experiments showed no change in the "foldedness" upon hydroxylation. Surface plasmon resonance measurements of binding to NFkappaB showed no difference in the NFkappaB binding kinetics or thermodynamics. Ubiquitin-independent proteasomal degradation experiments showed no difference in the half-life of the protein. Thus, it appears that hydroxylation of IkappaBalpha by FIH-1 is inconsequential, at least for the functions we could assay in vitro. |
