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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Related Experiment Video

Updated: Mar 26, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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The amyloid precursor protein (APP) binds the PIKfyve complex and modulates its function.

Heather Currinn1, Thomas Wassmer1

  • 1School of Life and Health Sciences, Aston University, Birmingham B4 7ET, U.K. currinnh@aston.ac.uk twassmer@hotmail.com.

Biochemical Society Transactions
|February 11, 2016
PubMed
Summary

The amyloid precursor protein (APP) interacts with the PIKfyve complex, regulating phosphoinositide metabolism. This discovery reveals a novel, beta-amyloid-independent pathway contributing to neurodegeneration in Alzheimer's disease.

Keywords:
5-bisphosphateAlzheimer's diseaseFab1Fig4PIKfyveVac14amyloid precursor proteinphosphatidylinositol-3trafficking

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Area of Science:

  • Cell biology
  • Neuroscience
  • Molecular biology

Background:

  • Phosphoinositides are crucial for membrane dynamics, cell signaling, and trafficking.
  • Dysregulation of phosphoinositides is linked to human diseases.
  • The PIKfyve complex regulates phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2) levels, vital for neuronal function.

Purpose of the Study:

  • To review the emerging regulation of the PIKfyve complex.
  • To highlight the novel interaction between APP and the PIKfyve complex.
  • To explore a potential beta-amyloid-independent mechanism in Alzheimer's disease pathogenesis.

Main Methods:

  • Literature review of phosphoinositide regulation and PIKfyve complex function.
  • Discussion of recent findings on APP interaction with the PIKfyve complex subunit Vac14.
  • Analysis of APP's role in modulating PIKfyve activity and PI(3,5)P2 dynamics.

Main Results:

  • The amyloid precursor protein (APP) directly interacts with Vac14, a subunit of the PIKfyve complex.
  • APP modulates the enzymatic activity of PIKfyve, affecting PI(3,5)P2 levels.
  • Loss of PIKfyve function leads to neurodegeneration, observed in mouse models and human patients.

Conclusions:

  • The APP gene family acts as a regulator of PI(3,5)P2 metabolism.
  • This interaction suggests a novel, beta-amyloid-independent mechanism contributing to neurodegeneration in Alzheimer's disease.
  • Further research into this pathway may reveal new therapeutic targets for Alzheimer's disease.