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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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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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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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Related Experiment Video

Updated: Mar 10, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Amyloid Precursor Proteins Are Dynamically Trafficked and Processed during Neuronal Development.

Jenna M Ramaker1, Robert S Cargill2, Tracy L Swanson3

  • 1Department of Cell, Developmental and Cancer Biology, Oregon Health and Science UniversityPortland, OR, USA; Neuroscience Graduate Program, Oregon Health and Science UniversityPortland, OR, USA.

Frontiers in Molecular Neuroscience
|December 10, 2016
PubMed
Summary
This summary is machine-generated.

Investigating the Amyloid Precursor Protein (APP) family in insects revealed that APPL protein is trafficked and processed in developing neurons. These findings offer new insights into APP protein regulation in the nervous system.

Keywords:
APPLD. melanogasterM. sextaamphisomemigrationoutgrowthsecretasetransport

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus
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Related Experiment Videos

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus
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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Amyloid Precursor Protein (APP) processing generates beta-amyloid (Aβ) fragments linked to Alzheimer's Disease (AD).
  • APP's role in neuronal development is complex due to mammalian orthologs (APLP1, APLP2).
  • Insects possess a single neuron-specific APP-like (APPL) protein, simplifying functional analysis.

Purpose of the Study:

  • To investigate the regulation of APPL trafficking and processing in neuronal development using insect models.
  • To understand how APPL cleavage fragments influence neuronal functions.
  • To compare APPL and APP trafficking and processing patterns.

Main Methods:

  • Utilized two insect models: Drosophila melanogaster and Manduca sexta.
  • Employed fluorescently tagged versions of APPL and APP for comparison with endogenous APPL.
  • Conducted in vitro and in vivo studies, including time-lapse imaging of double-tagged constructs.

Main Results:

  • Full-length APPL is trafficked to motile regions of developing neurons.
  • APPL is rapidly processed into N- and C-terminal fragments undergoing bi-directional transport.
  • APPL can be sequestered into amphisome-like compartments, and its cleavage impacts neuronal motility.
  • APP family protein trafficking and processing vary significantly across neuronal subtypes.

Conclusions:

  • Multiple mechanisms regulate APPL bioavailability to control nervous system responses.
  • APP family proteins exhibit complex, cell type-specific trafficking and processing patterns.
  • This study provides a new perspective on modulating APP family proteins for nervous system functions.