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Related Concept Videos

Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
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MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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PI3K/mTOR/AKT Signaling Pathway

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Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
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Related Experiment Video

Updated: May 15, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Neuronal PRRT3 coordinates amyloidogenic processing and Tau phosphorylation via distinct Ras-ERK-AP-1 and CaMKII/PP2A

Fei Chen1,2, Haohan Zhang2,3, Yaru Huang2

  • 1School of Life Science, Ningxia University, Yinchuan 750021, China.

Acta Biochimica Et Biophysica Sinica
|May 14, 2026
PubMed
Summary
This summary is machine-generated.

Researchers discovered proline-rich transmembrane protein 3 (PRRT3) as a key regulator in Alzheimer's disease (AD). Targeting PRRT3 may offer a novel strategy to address both amyloid-beta and tau pathologies in AD.

Keywords:
Alzheimer’s diseasePRRT3Tau phosphorylationcalcium signalingβ-amyloid

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Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

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Last Updated: May 15, 2026

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Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

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Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System
09:52

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Published on: December 28, 2017

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) pathology involves extracellular beta-amyloid (Aβ) and intracellular Tau hyperphosphorylation.
  • Upstream regulators coordinating these dual pathologies in AD remain largely unknown.

Purpose of the Study:

  • To identify novel upstream regulators of AD dual pathology.
  • To investigate the role of proline-rich transmembrane protein 3 (PRRT3) in AD pathogenesis.

Main Methods:

  • PRRT3 expression analysis in AD patient tissues and APP/PS1 mouse models.
  • PRRT3 knockdown experiments in neuronal cells to assess effects on amyloidogenic gene expression (APP, PS1, BACE1) and Aβ generation.
  • Investigation of PRRT3's mechanism involving AP-1 complex activation (c-Fos, c-Jun phosphorylation).
  • Transcriptomic profiling to analyze calcium signaling pathways and ERK activity.
  • Experiments using thapsigargin to manipulate intracellular calcium levels and assess reversal of PRRT3 knockdown effects on amyloid and Tau pathology.

Main Results:

  • PRRT3 expression is elevated in AD brains and persists in APP/PS1 mice.
  • PRRT3 knockdown reduces amyloidogenic gene expression, decreasing Aβ generation via AP-1 pathway activation.
  • PRRT3 knockdown attenuates calcium signaling and ERK activity, impacting Tau hyperphosphorylation by modulating CaMKII/PP2A balance.

Conclusions:

  • PRRT3 acts as a neuron-enriched upstream regulator linking calcium dysregulation to both amyloid processing and Tau phosphorylation in AD.
  • Targeting PRRT3 presents a potential therapeutic strategy for simultaneously addressing core pathological hallmarks of Alzheimer's disease.