The amyloid precursor protein (APP) binds the PIKfyve complex and modulates its function
نویسندگان
چکیده
منابع مشابه
The Amyloid Precursor Protein Controls PIKfyve Function
While the Amyloid Precursor Protein (APP) plays a central role in Alzheimer's disease, its cellular function still remains largely unclear. It was our goal to establish APP function which will provide insights into APP's implication in Alzheimer's disease. Using our recently developed proteo-liposome assay we established the interactome of APP's intracellular domain (known as AICD), thereby ide...
متن کاملThe Alzheimer Amyloid Precursor Protein (APP) and Fe65, an APP-Binding Protein, Regulate Cell Movement
FE65 binds to the Alzheimer amyloid precursor protein (APP), but the function of this interaction has not been identified. Here, we report that APP and FE65 are involved in regulation of cell movement. APP and FE65 colocalize with actin and Mena, an Abl-associated signaling protein thought to regulate actin dynamics, in lamellipodia. APP and FE65 specifically concentrate with beta 1-integrin in...
متن کاملPAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.
Understanding the intracellular transport of the beta-amyloid precursor protein (APP) is a major key to elucidate the regulation of APP processing and thus beta-amyloid peptide generation in Alzheimer disease pathogenesis. APP and its two paralogues, APLP1 and APLP2 (APLPs), are processed in a very similar manner by the same protease activities. A putative candidate involved in APP transport is...
متن کاملBinding of F-spondin to amyloid- precursor protein: A candidate amyloid- precursor protein ligand that modulates amyloid- precursor protein cleavage
Amyloidprecursor protein (APP), a type I membrane protein, is physiologically processed by or -secretases that cleave APP N-terminal to the transmembrane region. Extracellular -cleavage of APP generates a large secreted N-terminal fragment, and a smaller cellular C-terminal fragment. Subsequent -secretase cleavage in the transmembrane region of the C-terminal fragment induces secretion of small...
متن کاملThe Amyloid Precursor Protein (APP) Does Not Have a Ferroxidase Site in Its E2 Domain
The ubiquitous 24-meric iron-storage protein ferritin and multicopper oxidases such as ceruloplasmin or hephaestin catalyze oxidation of Fe(II) to Fe(III), using molecular oxygen as oxidant. The ferroxidase activity of these proteins is essential for cellular iron homeostasis. It has been reported that the amyloid precursor protein (APP) also has ferroxidase activity. The activity is assigned t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Society Transactions
سال: 2016
ISSN: 0300-5127,1470-8752
DOI: 10.1042/bst20150179