Shigeki Arawaka

TL;DR: Nicastrin and presenilins are likely to be functional components of a multimeric complex necessary for the intramembranous proteolysis of proteins such as Notch/GLP-1 and βAPP.

TL;DR: It is reported here that nicastrin is most probably a type 1 transmembrane glycoprotein that is expressed at moderate levels in the brain and in cultured neurons and that presenilin-1 interacts preferentially with mature Nicastrin, suggesting that correct trafficking and co-localization of the presenILin complex components are essential for activity.

TL;DR: Nicastrin has a similar role in processing Notch and βAPP, but the 312–369 domain may have differential effects on these activities, and it is reported that the Notch or βAPP pathways do not significantly compete with each other.

TL;DR: It is demonstrated that authentically Ser129-phosphorylated α-syn accelerates A53T α-Syn neurotoxicity without the formation of detergent-insoluble α- syn, and suggests that the degenerative process could be constrained by inhibiting the kinase that phosphorylates α- Syn at Ser129.

TL;DR: It is reported here that specific mutations in the N terminus, loop, or C terminus of PS1 all increase the production of Aβ42 but cause inhibition of both ε-secretase cleavage of APP and S3-cleavage of Notch.