ArticleThe Journal of biological chemistry2011
A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- TrkB receptor cleavage by delta-secretase abolishes its phosphorylation of APP, aggravating Alzheimer's disease pathologies.Molecular psychiatry · 2021Article
- Article
- Article
- Not just amyloid: physiological functions of the amyloid precursor protein family.Nature reviews. Neuroscience · 2017Review
- APP Protein Family Signaling at the Synapse: Insights from Intracellular APP-Binding Proteins.Frontiers in molecular neuroscience · 2017Review
- 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.The Journal of biological chemistry · 2016Article
- FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.Scientific reports · 2016Article
- Review
- APP Is a Context-Sensitive Regulator of the Hippocampal Presynaptic Active Zone.PLoS computational biology · 2016Article
- The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Article
- APP intracellular domain acts as a transcriptional regulator of miR-663 suppressing neuronal differentiation.Cell death & disease · 2015Article
- The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes.Acta neuropathologica · 2015Review
- Y682G Mutation of Amyloid Precursor Protein Promotes Endo-Lysosomal Dysfunction by Disrupting APP-SorLA Interaction.Frontiers in cellular neuroscience · 2015Article
- Article
- Neprilysin and Aβ Clearance: Impact of the APP Intracellular Domain in NEP Regulation and Implications in Alzheimer's Disease.Frontiers in aging neuroscience · 2013Review
- A new molecular explanation for age-related neurodegeneration: the Tyr682 residue of amyloid precursor protein.BioEssays : news and reviews in molecular, cellular and developmental biology · 2013Article
- Turnover of amyloid precursor protein family members determines their nuclear signaling capability.PloS one · 2013Article
- Tyr682 in the Aβ-precursor protein intracellular domain regulates synaptic connectivity, cholinergic function, and cognitive performance.Aging cell · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The Aβ-precursor protein (APP) intracellular domain is highly conserved and contains many potentially important residues, in particular the (682)YENPTY(687) motif. To dissect the functions of this sequence in vivo, we created an APP knock-in allele mutating Tyr(682) to Gly (Y682G). Crossing this allele to APP-like protein 2 (APLP2) knock-out background showed that mutation of Tyr(682) results in postnatal lethality and neuromuscular synapse defects similar to doubly deficient APP/APLP2 mice. Our results demonstrate that a single residue in the APP intracellular region, Tyr(682), is indispensable for the essential function of APP in developmental regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.