Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.

Scientific reports - 11 May 2016

Strecker Paul, Ludewig Susann, Rust Marco, Mundinger Tabea A, Görlich Andreas, Krächan Elisa G, Mehrfeld Christina, Herz Joachim, Korte Martin, Guénette Suzanne Y, Kins Stefan

Abstract excerpt

The FE65 adaptor proteins (FE65, FE65L1 and FE65L2) bind proteins that function in diverse cellular pathways and are essential for specific biological processes. Mice lacking both FE65 and FE65L1 exhibit ectopic neuronal positioning in the cortex and muscle weakness. p97FE65-KO mice, expressing a shorter FE65 isoform able to bind amyloid precursor protein family members (APP, APLP1, APLP2), develop defective...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anxiety
Share to Dendritic Spines

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Learning

Share to Long-Term Potentiation

Share to Maze Learning

Share to Memory Disorders

Share to Neuromuscular Junction

Share to Pyramidal Cells

Source

Open in PubMed Open full text

Identifiers

PMID: 27734846
DOI: 10.1038/srep25652
PMCID: PMC4899880

Genes

APLP2
APP
APLP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.PMID 27734846Read ↗

The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation.Semantic proximity Read ↗

Loss of all three APP family members during development impairs synaptic function and plasticity, disrupts learning, and causes an autism-like phenotype.Semantic proximity Read ↗

The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior.Semantic proximity Read ↗

The role of APP and APLP for synaptic transmission, plasticity, and network function: lessons from genetic mouse modelsSemantic proximity Read ↗

Proteins implicated in Alzheimer disease. The role of FE65, a new adapter which binds to beta-amyloid precursor protein.Semantic proximity Read ↗

Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2.Semantic proximity Read ↗

APP and APLP2 are essential at PNS and CNS synapses for transmission, spatial learning and LTPSemantic proximity Read ↗

A Neuroligin-1 mutation associated with Alzheimer’s disease produces memory and age-dependent impairments in hippocampal plasticitySemantic proximity Read ↗

Early Disruption of Synaptic Function, Impairment of Plasticity, and Decreased of Cortical Circuit Connectivity in an Alzheimer’S Mouse Model of Amyloid DepositionSemantic proximity Read ↗

Age-related impairment of synaptic transmission but normal long-term potentiation in transgenic mice that overexpress the human APP695SWE mutant form of amyloid precursor protein.Semantic proximity Read ↗

Age-related synaptic dysfunction in Tg2576 mice starts as a failure in early long-term potentiation which develops into a full abolishment of late long-term potentiation.Semantic proximity Read ↗

feh-1 and apl-1, the Caenorhabditis elegansorthologues of mammalian Fe65 and β-amyloid precursor protein genes, are involved in the same pathway that controls nematode pharyngeal pumpingSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.