| First Author | Song WJ | Year | 2013 |
| Journal | Neurosci Lett | Volume | 554 |
| Pages | 135-40 | PubMed ID | 24021800 |
| Mgi Jnum | J:201827 | Mgi Id | MGI:5515841 |
| Doi | 10.1016/j.neulet.2013.08.066 | Citation | Song WJ, et al. (2013) Dyrk1A-mediated phosphorylation of RCAN1 promotes the formation of insoluble RCAN1 aggregates. Neurosci Lett 554:135-40 |
| abstractText | The mechanisms underlying aggregate formation in age-related neurodegenerative diseases remain not well understood. Here we investigated whether dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 1A (Dyrk1A) is involved in the formation of regulator of calcineurin 1 (RCAN1) aggregates. We show that RCAN1 self-associates and forms multimers, and that this process is promoted by the Dyrk1A-mediated phosphorylation of RCAN1 at the Thr(192) residue. Transgenic mice that overexpress the Dyrk1A exhibited lower levels of phospho-Thr(192)-RCAN1 in 10-month-old-group compared to littermate controls, when analyzed with soluble hippocampus lysates. These results suggest that the phosphorylation of RCAN1 by Dyrk1A stimulates the formation of insoluble aggregates upon aging. |
