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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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Amyloid Fibrils03:03

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PI3K/mTOR/AKT Signaling Pathway01:22

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Related Experiment Video

Updated: Apr 8, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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The Amyloid Precursor Protein Controls PIKfyve Function.

Zita Balklava1, Christian Niehage2, Heather Currinn1

  • 1Aston University, School of Life and Health Sciences, Aston Triangle, Birmingham, B4 7ET, United Kingdom.

Plos One
|July 1, 2015
PubMed
Summary
This summary is machine-generated.

Amyloid Precursor Protein (APP) regulates endosomal function by interacting with the PIKfyve complex. This discovery offers new insights into Alzheimer's disease mechanisms and neuronal health.

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Related Experiment Videos

Last Updated: Apr 8, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • The cellular function of Amyloid Precursor Protein (APP) is not fully understood, despite its central role in Alzheimer's disease.
  • Investigating APP's function is crucial for understanding its implications in Alzheimer's disease pathogenesis.

Purpose of the Study:

  • To elucidate the cellular function of APP by identifying its interactors.
  • To gain mechanistic insights into APP's role in cellular processes and Alzheimer's disease.

Main Methods:

  • Utilized a novel proteo-liposome assay to determine the interactome of APP's intracellular domain (AICD).
  • Employed a combination of biochemical, cell biological, and genetic approaches for validation.
  • Conducted studies using C. elegans genetics to assess in vivo function.

Main Results:

  • Identified the PIKfyve complex as a novel interactor of APP.
  • Demonstrated that APP binds to PIKfyve, a kinase essential for phosphatidylinositol-3,5-bisphosphate synthesis.
  • Showcased that APP functionally cooperates with PIKfyve in vivo, maintaining endosomal and neuronal function.

Conclusions:

  • Established an unexpected role for APP in regulating endosomal phosphoinositide metabolism.
  • Highlighted the critical importance of the APP-PIKfyve interaction for endosomal homeostasis and neuronal function.
  • Provided significant implications for understanding Alzheimer's disease, linking APP to endosomal dysfunction.