| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2049815 | FEBS Letters | 2008 | 4 Pages |
Myelin basic protein (MBP) from multiple sclerosis (MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.Structured summaryMINT-6613181:MAPK (uniprotkb:P28482) phosphorylates (MI:0217) MBP (uniprotkb:P02687) by protein kinase assay (MI:0424)MINT-6613171, MINT-6613190:MAPK (uniprotkb:P28482) phosphorylates (MI:0217) U24 (uniprotkb:Q69559) by protein kinase assay (MI:0424)
