Phosphorylation of a Tyrosine in the Amyloid-β Protein Precursor Intracellular Domain Inhibits Fe65 Binding and Signaling

No abstract is available for this paper.

• Publication year

  2009

• Venue

  Journal of Alzheimer's Disease

• Publication date

  2009-02-16

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.3233/JAD-2009-0970PMID 19221419
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The FE65 proteins and Alzheimer's disease

  2008cited by this paper
• The gamma/epsilon-secretase-derived APP intracellular domain fragments regulate p53.

  2007cited by this paper
• Essential roles for the FE65 amyloid precursor protein‐interacting proteins in brain development

  2006cited by this paper
• Presenilin-dependent transcriptional control of the Abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP.

  2005cited by this paper
• Activation of GSK-3 and phosphorylation of CRMP2 in transgenic mice expressing APP intracellular domain

  2005cited by this paper
• Faculty Opinions recommendation of Presenilin-dependent transcriptional control of the Abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP.

  2005cited by this paper
• Adaptor protein interactions: modulators of amyloid precursor protein metabolism and Alzheimer's disease risk?

  2004cited by this paper
• Dissection of Amyloid-β Precursor Protein-dependent Transcriptional Transactivation*

  2004cited by this paper
• Faculty Opinions recommendation of Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation.

  2004cited by this paper
• Growth Factor Receptor-bound Protein 2 Interaction with the Tyrosine-phosphorylated Tail of Amyloid β Precursor Protein Is Mediated by Its Src Homology 2 Domain*

  2004influential reference
• JNK-interacting protein-1 promotes transcription of A beta protein precursor but not A beta precursor-like proteins, mechanistically different than Fe65.

  2003cited by this paper
• SH2 and PTB Domains in Tyrosine Kinase Signaling

  2003cited by this paper
• The Amyloid Precursor Protein and Its Regulatory Protein, FE65, in Growth Cones and Synapses In Vitro and In Vivo

  2003cited by this paper
• Amyloid (cid:1) Protein Precursor Is Phosphorylated by JNK-1 Independent of, yet Facilitated by, JNK-Interacting Protein (JIP)-1*

  2003cited by this paper
• APP processing is regulated by cytoplasmic phosphorylation

  2003cited by this paper
• Tyrosine Phosphorylation of the β-Amyloid Precursor Protein Cytoplasmic Tail Promotes Interaction with Shc*

  2002influential reference
• A physiologic signaling role for the gamma -secretase-derived intracellular fragment of APP.

  2002cited by this paper
• A candidate molecular mechanism for the association of an intronic polymorphism of FE65 with resistance to very late onset dementia of the Alzheimer type.

  2002cited by this paper
• Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein.

  2002cited by this paper
• The β-Amyloid Precursor Protein Functions as a Cytosolic Anchoring Site That Prevents Fe65 Nuclear Translocation*

  2001cited by this paper
• The Intracellular Domain of the β-Amyloid Precursor Protein Is Stabilized by Fe65 and Translocates to the Nucleus in a Notch-like Manner*

  2001cited by this paper
• A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60.

  2001cited by this paper
• Amino-terminal modification and tyrosine phosphorylation of [corrected] carboxy-terminal fragments of the amyloid precursor protein in Alzheimer's disease and Down's syndrome brain.

  2001cited by this paper
• The β-Amyloid Precursor Protein APP Is Tyrosine-phosphorylated in Cells Expressing a Constitutively Active Form of the Abl Protoncogene*

  2001cited by this paper
• c-Jun N-Terminal Kinase (JNK)-Interacting Protein-1b/Islet-Brain-1 Scaffolds Alzheimer's Amyloid Precursor Protein with JNK

  2001cited by this paper
• Short Communication FE65 in Alzheimer’s Disease Neuronal Distribution and Association with Neurofibrillary Tangles

  2001cited by this paper
• The Disabled 1 Phosphotyrosine-Binding Domain Binds to the Internalization Signals of Transmembrane Glycoproteins and to Phospholipids

  1999cited by this paper
• Regulation of β-Amyloid Secretion by FE65, an Amyloid Protein Precursor-binding Protein*

  1999cited by this paper
• Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer’s Amyloid Precursor Protein*

  1999cited by this paper
• Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein.

  1998cited by this paper
• The Fe65 Adaptor Protein Interacts through Its PID1 Domain with the Transcription Factor CP2/LSF/LBP1*

  1998cited by this paper
• The Cytoplasmic Domain of Alzheimer’s Amyloid Precursor Protein Is Phosphorylated at Thr654, Ser655, and Thr668 in Adult Rat Brain and Cultured Cells

  1997cited by this paper
• Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein.

  1996cited by this paper
• The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein

  1996cited by this paper
• The Regions of the Fe65 Protein Homologous to the Phosphotyrosine Interaction/Phosphotyrosine Binding Domain of Shc Bind the Intracellular Domain of the Alzheimer's Amyloid Precursor Protein (*)

  1995cited by this paper
• Cell cycle‐dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein.

  1994cited by this paper
• Signal-dependent membrane protein trafficking in the endocytic pathway.

  1993cited by this paper

• The AICD interactome: implications in neurodevelopment and neurodegeneration

  2024cites this paper
• Phosphorylation and Glycosylation of Amyloid-β Protein Precursor: The Relationship to Trafficking and Cleavage in Alzheimer’s Disease

  2021cites this paper
• Fyn Tyrosine Kinase Elicits Amyloid Precursor Protein Tyr682 Phosphorylation in Neurons from Alzheimer’s Disease Patients

  2020cites this paper
• The Y682ENPTY687 motif of APP: Progress and insights toward a targeted therapy for Alzheimer's disease patients.

  2019cites this paper
• A fluorescent protein-readout for transcriptional activity reveals regulation of APP nuclear signaling by phosphorylation sites

  2019cites this paper
• The amyloid-β precursor protein (APP)-binding protein Fe65 and APP processing

  2018cites this paper
• Small things matter: Implications of APP intracellular domain AICD nuclear signaling in the progression and pathogenesis of Alzheimer's disease

  2017cites this paper
• Implication du domaine intracellulaire du précurseur de la protéine amyloïde dans la modulation de la plasticité synaptique

  2016influential citation
• Nuclear spheres modulate the expression of BEST1 and GADD45G.

  2016cites this paper
• Amyloid Precursor Protein (APP) May Act as a Substrate and a Recognition Unit for CRL4CRBN and Stub1 E3 Ligases Facilitating Ubiquitination of Proteins Involved in Presynaptic Functions and Neurodegeneration*

  2016cites this paper
• c-Abl links APP-BACE1 interaction promoting APP amyloidogenic processing in Niemann-Pick type C disease.

  2016cites this paper
• Y682G Mutation of Amyloid Precursor Protein Promotes Endo-Lysosomal Dysfunction by Disrupting APP–SorLA Interaction

  2015influential citation
• Cellular functions of the amyloid precursor protein from development to dementia.

  2015cites this paper
• Vascular Dysfunction Associated with Type 2 Diabetes and Alzheimer’s Disease: A Potential Etiological Linkage

  2014cites this paper
• APP Is Cleaved by Bace1 in Pre-Synaptic Vesicles and Establishes a Pre-Synaptic Interactome, via Its Intracellular Domain, with Molecular Complexes that Regulate Pre-Synaptic Vesicles Functions

  2014cites this paper
• Integrating Data for Modeling Biological Complexity

  2014cites this paper
• A role for amyloid precursor proteins in regulating neuronal motility

  2013influential citation
• A new molecular explanation for age-related neurodegeneration: The Tyr682 residue of amyloid precursor protein

  2013cites this paper
• An Intracellular Threonine of Amyloid-β Precursor Protein Mediates Synaptic Plasticity Deficits and Memory Loss

  2013cites this paper
• 1H, 13C, and 15N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65

  2013influential citation
• Amyloid Beta A4 Precursor Protein-binding Family B Member 1 (FE65) Interactomics Revealed Synaptic Vesicle Glycoprotein 2A (SV2A) and Sarcoplasmic/Endoplasmic Reticulum Calcium ATPase 2 (SERCA2) as New Binding Proteins in the Human Brain*

  2013cites this paper
• Visualization and Quantification of APP Intracellular Domain-Mediated Nuclear Signaling by Bimolecular Fluorescence Complementation

  2013cites this paper
• Alzheimer's Disease-Related Loss of Pin1 Function Influences the Intracellular Localization and the Processing of AβPP

  2012cites this paper
• Relationships between the amyloid precursor protein and its various proteolytic fragments and neuronal systems

  2012cites this paper
• The physiology of the β‐amyloid precursor protein intracellular domain AICD

  2012cites this paper
• Tyr682 in the Aβ‐precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance

  2012cites this paper
• Functional implications of the conformational switch in AICD peptide upon binding to Grb2-SH2 domain.

  2011cites this paper
• A Persistent Stress Response to Impeded Axonal Transport Leads to Accumulation of Amyloid-β in the Endoplasmic Reticulum, and Is a Probable Cause of Sporadic Alzheimer’s Disease

  2011cites this paper
• APP physiological and pathophysiological functions: insights from animal models

  2011cites this paper
• The Intracellular Threonine of Amyloid Precursor Protein That Is Essential for Docking of Pin1 Is Dispensable for Developmental Function

  2011cites this paper
• APP is Phosphorylated by TrkA and Regulates NGF/TrkA Signaling

  2011cites this paper
• A Single Tyrosine Residue in the Amyloid Precursor Protein Intracellular Domain Is Essential for Developmental Function*

  2011cites this paper
• Uncovering Molecular Biomarkers That Correlate Cognitive Decline with the Changes of Hippocampus' Gene Expression Profiles in Alzheimer's Disease

  2010cites this paper
• Tyr682 in the Intracellular Domain of APP Regulates Amyloidogenic APP Processing In Vivo

  2010cites this paper
• Proteolytic processing of the Alzheimer APP protein family during neuronal differentiation

  2009influential citation
• The interactome of the amyloid β precursor protein family members is shaped by phosphorylation of their intracellular domains

  2009cites this paper