Vesicle Transport: A New Player in APP Trafficking
نویسندگان
چکیده
The trafficking of the amyloid precursor protein (APP) is critical for controlling the generation of the toxic A beta peptide that is central to amyloid formation in Alzheimer's disease. A new study reveals a key role for the AP4 adaptor protein complex in the Golgi-to-endosome trafficking of APP.
منابع مشابه
Subcellular trafficking of the amyloid precursor protein gene family and its pathogenic role in Alzheimer's disease.
Changes in the intracellular transport of amyloid precursor protein (APP) affect the extent to which APP is exposed to alpha- or beta-secretase in a common subcellular compartment and therefore directly influence the degree to which APP undergoes the amyloidogenic pathway leading to generation of beta-amyloid. As the presynaptic regions of neurons are thought to be the main source of beta-amylo...
متن کاملOptic Nerve Degeneration and Ageing
Major pathological hallmarks of Alzheimer Disease are insoluble deposits of the short amyloid β-peptide (β-amyloid, Aβ), which is derived by sequential proteolytic cleavage from a large type I trans-membrane protein, the β-amyloid precursor protein (APP). APP is anterogradely transported by fast axonal transport in a distinct transport vesicle, but both the biochemical composition of such a ves...
متن کاملCoordinated transport of phosphorylated amyloid-β precursor protein and c-Jun NH2-terminal kinase–interacting protein-1
The transmembrane protein amyloid-beta precursor protein (APP) and the vesicle-associated protein c-Jun NH(2)-terminal kinase-interacting protein-1 (JIP-1) are transported into axons by kinesin-1. Both proteins may bind to kinesin-1 directly and can be transported separately. Because JIP-1 and APP can interact, kinesin-1 may recruit them as a complex, enabling their cotransport. In this study, ...
متن کاملUncoupled packaging of amyloid precursor protein and presenilin 1 into coat protein complex II vesicles.
Mutant forms of presenilin (PS) 1 and 2 and amyloid precursor protein (APP) lead to familial Alzheimer's disease. Several reports indicate that PS may modulate APP export from the endoplasmic reticulum (ER). To develop a test of this possibility, we reconstituted the capture of APP and PS1 in COPII (coat protein complex II) vesicles formed from ER membranes in permeabilized cultured cells. The ...
متن کاملAlzheimer's presenilin 1 is a putative membrane receptor for rab GDP dissociation inhibitor.
Mutations in the presenilin 1 ( PS-1 ) gene cause Alzheimer's disease (AD). These mutations alter the processing of the amyloid precursor protein (APP) by increasing the production of the fibrillogenic amyloid fragment, Abeta1-42/43. Since the secretase activities that process APP are localized in different intracellular compartments, it is likely that membrane transport is a key factor in the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Current Biology
دوره 20 شماره
صفحات -
تاریخ انتشار 2010