Abstract:
: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.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Song WJ,Song EA,Choi SH,Baik HH,Jin BK,Kim JH,Chung SHdoi
10.1016/j.neulet.2013.08.066subject
Has Abstractpub_date
2013-10-25 00:00:00pages
135-40eissn
0304-3940issn
1872-7972pii
S0304-3940(13)00799-4journal_volume
554pub_type
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