Abstract:
:Alpha synuclein (α-syn) is a central player in neurodegeneration, but the mechanisms triggering its pathology are not fully understood. Here we found that α-syn is a highly efficient substrate for arginyltransferase ATE1 and is arginylated in vivo by a novel mid-chain mechanism that targets the acidic side chains of E46 and E83. Lack of arginylation leads to increased α-syn aggregation and causes the formation of larger pathological aggregates in neurons, accompanied by impairments in its ability to be cleared via normal degradation pathways. In the mouse brain, lack of arginylation leads to an increase in α-syn's insoluble fraction, accompanied by behavioral changes characteristic for neurodegenerative pathology. Our data show that lack of arginylation in the brain leads to neurodegeneration, and suggests that α-syn arginylation can be a previously unknown factor that facilitates normal α-syn folding and function in vivo.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Wang J,Han X,Leu NA,Sterling S,Kurosaka S,Fina M,Lee VM,Dong DW,Yates JR 3rd,Kashina Adoi
10.1038/s41598-017-11713-zsubject
Has Abstractpub_date
2017-09-12 00:00:00pages
11323issue
1issn
2045-2322pii
10.1038/s41598-017-11713-zjournal_volume
7pub_type
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