Cited by 1,202Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60

Cao, Xinwei, Südhof, Thomas C.·2001·Science

Abstract

Amyloid-beta precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the transmembrane region by gamma-secretase. gamma-Cleavage of APP produces the extracellular amyloid beta-peptide of Alzheimer's disease and releases an intracellular tail fragment of unknown physiological function. We now demonstrate that the cytoplasmic tail of APP forms a multimeric complex with the nuclear adaptor protein Fe65 and the histone acetyltransferase Tip60. This complex potently stimulates transcription via heterologous Gal4- or LexA-DNA binding domains, suggesting that release of the cytoplasmic tail of APP by gamma-cleavage may function in gene expression.

Integrity signals

Registry

Crossref · 10.1126/science.1058783

Cites

36 of 36 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Presenilin-mediated cleavage of APP releases APP intracellular domain (ICD), which is thought to participate in signaling pathways via association with Fe65 and Tip60.

    “The presenilin-mediated cleavage of APP occurs within the transmembrane domain and releases the APP intracellular domain (ICD), which is thought to participate in signaling pathways via association with the adaptor protein Fe65 and the histone acetyltransferase Tip60 (Cao and Sudhof, 2001).”
  • Fe65 contains a WW domain, is expressed in the brain, associates with APP via a PTB domain and modulates its signaling properties.

    “Fe65, which contains a WW domain, is expressed in the brain and associates with APP via a PTB domain and modulates it’s signaling properties (Cao and Sudhof, 2001).”

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Cao, X., & Südhof, T. C.
Affiliations
  • Howard Hughes Medical Institute (US)
  • The Center for Basic Neuroscience, Department of Molecular Genetics, and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, TX 75390–9111 USA.
Venue
Science
Published
2001-07-06
Volume
293
Issue
5527
Pages
115-120
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1988986946
Cited by
1,202
References
36
Citations by year
2026: 12 · 2025: 11 · 2024: 7 · 2023: 14 · 2022: 21 · 2021: 21 · 2020: 21 · 2019: 17 · 2018: 25 · 2017: 31 · 2016: 34 · 2015: 35 · 2014: 55 · 2013: 52 · 2012: 57
FWCI
55.90
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
amyloid precursor protein, Fe65, Tip60, histone acetyltransferase, transcriptional activation, gamma-secretase cleavage, Alzheimer's disease, nuclear complex, gene expression regulation
MeSH terms
Lysine Acetyltransferase 5, LexA Repressor Protein, Acetyltransferases, Animals, Bacterial Proteins, Cell Line, DNA-Binding Proteins, Fungal Proteins, Humans, Mutation, Nerve Tissue Proteins, Nuclear Proteins, Peptide Fragments, Endopeptidases, Plasmids, Precipitin Tests, Protein Binding, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Serine Endopeptidases, Transcription Factors, Transcription, Genetic, Transfection, Transcriptional Activation, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Protein Structure, Tertiary, Two-Hybrid System Techniques, Protein Transport, Saccharomyces cerevisiae Proteins, Macromolecular Substances, Rats, Histone Acetyltransferases, Amyloid Precursor Protein Secretases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review