Alpha synuclein (-syn) is  a  central  player in neurodegeneration,
   but  the  mechanisms  triggering  its   pathology   are  not  fully
   understood.   Here  we  found  that  -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  -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 -syns 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 -syn arginylation  can  be  a  previously  unknown factor that
   facilitates normal -syn folding and function in vivo.

   (Scientific Reports, Volume 7, 11323,
    doi:10.1038/s41598-017-11713-z, 2017)