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Related Concept Videos

Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Rab Cascades01:25

Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
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SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Updated: Nov 28, 2025

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
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Soluble 4R0N Tau Abrogates Endocytic Vesicular Dynamics.

Tharun Selvam Mahendran1, S N Suresh2, Lakshmi Garimella1

  • 1Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Bangalore, India.

Frontiers in Aging Neuroscience
|November 30, 2020
PubMed
Summary

Soluble tau disrupts endolysosomal and autophagic pathways, impacting amyloid precursor protein (APP) trafficking. This suggests a novel mechanism by which soluble tau may contribute to Alzheimer's disease pathogenesis.

Keywords:
Alzheimer’s diseaseamyloid precursor protein (APP)autophagic stressendocytic dysfunctionendosome dysfunctionsoluble 4R0N tauvesicle trackingvesicular trafficking

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Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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Author Spotlight: Understanding the Impact of Pathological Proteins on Axonal Transport in Neurodegenerative Diseases
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Author Spotlight: Understanding the Impact of Pathological Proteins on Axonal Transport in Neurodegenerative Diseases

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Author Spotlight: Understanding the Impact of Pathological Proteins on Axonal Transport in Neurodegenerative Diseases
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Author Spotlight: Understanding the Impact of Pathological Proteins on Axonal Transport in Neurodegenerative Diseases

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Aggregated tau is a key feature in neurodegenerative diseases, but its pathogenic role is debated.
  • Soluble tau's specific contribution to molecular pathogenesis, particularly in Alzheimer's disease (AD) endolysosomal and autophagic dysfunction, remains unclear.

Purpose of the Study:

  • To investigate the impact of soluble 4R0N tau overexpression on endolysosomal and autophagic pathways.
  • To determine how soluble tau affects the trafficking and localization of amyloid precursor protein (APP).

Main Methods:

  • Overexpression of soluble 4R0N tau in cellular models.
  • Analysis of endolysosomal and autophagic marker expression.
  • Live-cell imaging to assess vesicular dynamics.
  • Tracking of APP localization within the endocytic pathway.

Main Results:

  • Soluble 4R0N tau overexpression altered expression of endolysosomal and autophagic markers.
  • Live-cell imaging revealed impaired early endosome dynamics and maturation.
  • APP was found to preferentially localize to endocytic compartments involved in amyloidogenic processing.

Conclusions:

  • Soluble 4R0N tau disrupts endolysosomal system dynamics and autophagy.
  • Altered APP trafficking suggests a potential modulation of amyloid-beta (Aβ) generation.
  • These findings highlight soluble tau's role in early AD pathogenesis.