scholarly journals The Intracellular Domain of the β-Amyloid Precursor Protein Is Stabilized by Fe65 and Translocates to the Nucleus in a Notch-like Manner

2001 ◽  
Vol 276 (43) ◽  
pp. 40288-40292 ◽  
Author(s):  
W. Taylor Kimberly ◽  
Jessica B. Zheng ◽  
Suzanne Y. Guénette ◽  
Dennis J. Selkoe
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Intracellular Domain ◽  
Β Amyloid

scholarly journals Insulin-degrading Enzyme Rapidly Removes the β-Amyloid Precursor Protein Intracellular Domain (AICD)

2002 ◽  
Vol 277 (16) ◽  
pp. 13389-13393 ◽  
Author(s):  
Dieter Edbauer ◽  
Michael Willem ◽  
Sven Lammich ◽  
Harald Steiner ◽  
Christian Haass
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Insulin Degrading Enzyme ◽  
Intracellular Domain ◽  
Degrading Enzyme ◽  
Β Amyloid

scholarly journals Pharmacological targeting of the β-amyloid precursor protein intracellular domain

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Caterina Branca ◽  
Ilenia Sarnico ◽  
Roberta Ruotolo ◽  
Annamaria Lanzillotta ◽  
Arturo Roberto Viscomi ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Intracellular Domain ◽  
Β Amyloid

O4-04-06 β-Amyloid precursor protein intracellular domain (AICD) strongly enhances resting free cytosolic calcium levels

2004 ◽  
Vol 25 ◽  
pp. S81
Author(s):  
Runa Hamid ◽  
Michael Willem ◽  
Dieter Edbauer ◽  
Harald Steiner ◽  
Ulrike Müller ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Cytosolic Calcium ◽  
Precursor Protein ◽  
Intracellular Domain ◽  
Β Amyloid

scholarly journals Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's β-amyloid precursor protein

1998 ◽  
Vol 330 (1) ◽  
pp. 513-519 ◽  
Author(s):  
Angela DUILIO ◽  
Raffaella FARAONIO ◽  
Giuseppina MINOPOLI ◽  
Nicola ZAMBRANO ◽  
Tommaso RUSSO
Keyword(s):  
Amyloid Precursor Protein ◽  
Protein Interaction ◽  
Protein Family ◽  
Precursor Protein ◽  
Protein Isoforms ◽  
Rat Tissues ◽  
Interaction Domain ◽  
Intracellular Domain ◽  
Protein Protein Interaction ◽  
Β Amyloid

We previously demonstrated that Fe65 protein is one of the ligands of the cytoplasmic domain of β-amyloid precursor protein (APP). Another ligand of this molecule was recently identified; it is similar to Fe65, so it was named Fe65-like (Fe65L1). Herein we describe the cloning of another Fe65-like cDNA (Fe65L2), similar to Fe65 and to Fe65L1, which encodes a protein of approx. 50 kDa. Its cognate mRNA is expressed in various rat tissues, particularly in brain and testis. The three members of the Fe65 protein family share several structural and functional characteristics. The primary structures of the three proteins can be aligned in three regions corresponding to the protein-protein interaction domains of Fe65 [the protein-protein interaction domain containing two conserved tryptophan residues and the two phosphotyrosine interaction domain/phosphotyrosine binding (PID/PTB) domains], whereas the remaining sequences are poorly related. Like Fe65, Fe65L1 and Fe65L2 genes encode two different protein isoforms, derived from the alternative splicing of a very small exon of only six nucleotides, which results, within the N-terminal PID/PTB domain, in the presence or absence of two acidic/basic amino acids. Fe65L2 is able to interact, both in vitro and in vivo, with the intracellular domain of APP. Also, in the case of APP, another two closely related proteins exist, named β-amyloid precursor-like protein (APLP)1 and APLP2: by using the interaction trap procedure we observed that both Fe65 and Fe65L2 interact with APP, APLP1 or APLP2, although with different efficiencies.

scholarly journals Fe65 Stimulates Proteolytic Liberation of the β-Amyloid Precursor Protein Intracellular Domain

2007 ◽  
Vol 282 (46) ◽  
pp. 33313-33325 ◽  
Author(s):  
Jesse C. Wiley ◽  
Elise A. Smith ◽  
Mark P. Hudson ◽  
Warren C. Ladiges ◽  
Mark Bothwell
Keyword(s):  
Amyloid Precursor Protein ◽  
Proteolytic Processing ◽  
Precursor Protein ◽  
Direct Stimulation ◽  
Intracellular Domain ◽  
App Processing ◽  
Nuclear Signaling ◽  
Enhanced Production ◽  
Β Amyloid ◽  
Stimulation Of

The β-amyloid precursor protein (APP)-binding protein Fe65 is involved in APP nuclear signaling and several steps in APP proteolytic processing. In this study, we show that Fe65 stimulates γ-secretase-mediated liberation of the APP intracellular domain (AICD). The mechanism of Fe65-mediated stimulation of AICD formation appears to be through enhanced production of the carboxyl-terminal fragment substrates of γ-secretase and direct stimulation of processing by γ-secretase. The stimulatory capacity of Fe65 is isoform-dependent, as the non-neuronal and a2 isoforms promote APP processing more effectively than the exon 9 inclusive neuronal form of Fe65. Intriguingly, Fe65 stimulation of AICD production appears to be inversely related to pathogenic β-amyloid production as the Fe65 isoforms profoundly stimulate AICD production and simultaneously decrease Aβ42 production. Despite the capacity of Fe65 to stimulate γ-secretase-mediated APP proteolysis, it does not rescue the loss of proteolytic function associated with the presenilin-1 familial Alzheimer disease mutations. These data suggest that Fe65 regulation of APP proteolysis may be integrally associated with its nuclear signaling function, as all antecedent proteolytic steps prior to release of Fe65 from the membrane are fostered by the APP-Fe65 interaction.

β-Amyloid precursor protein metabolism: focus on the functions and degradation of its intracellular domain

2010 ◽  
Vol 62 (4) ◽  
pp. 308-317 ◽  
Author(s):  
Erica Buoso ◽  
Cristina Lanni ◽  
Gennaro Schettini ◽  
Stefano Govoni ◽  
Marco Racchi
Keyword(s):  
Amyloid Precursor Protein ◽  
Protein Metabolism ◽  
Precursor Protein ◽  
Intracellular Domain ◽  
Amyloid Precursor Protein Metabolism ◽  
Β Amyloid
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