Abstract
Alzheimer's disease is characterized pathologically by senile plaques in the brain. The major component of senile plaques is amyloid-beta (Abeta), which is cleaved from Alzheimer's Abeta protein precursor (AbetaPP). Recently, information regarding the cytoplasmic tail of AbetaPP has started to emerge, opening up various insights into the physiological roles of AbetaPP and its pathological role in Alzheimer's disease. The cytoplasmic domain of AbetaPP shares the evolutionarily conserved GYENPTY motif, which binds to a number of adaptor proteins containing the phosphotyrosine interaction domain (PID). Among the PID-containing proteins, this article focuses on four groups of adaptor proteins of AbetaPP: Fe65, X11, mDab1, and c-Jun N-terminal kinase-interacting protein 1b/islet-brain 1.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
