Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

6.0K
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...
6.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

STIP1/HOP promotes the formation of cytotoxic α-synuclein oligomers.

Molecular neurodegeneration advances·2026
Same author

An automated workflow for quantifying the formation of synuclein aggregates in human dopaminergic neurons.

Methods (San Diego, Calif.)·2026
Same author

N-terminal acetylation reduces synuclein pathology in models of Parkinson's disease.

Neurobiology of disease·2026
Same author

Cell type transcriptomic modules reveal shared molecular mechanisms in Alzheimer's and Parkinson's disease.

GigaScience·2026
Same author

A high-content imaging workflow to screen for molecules that reduce cellular uptake of α-synuclein preformed fibrils.

Methods (San Diego, Calif.)·2026
Same author

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Mar 7, 2026

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
09:12

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

6.8K

Rab7A regulates tau secretion.

Lilia Rodriguez1,2,3, Nguyen-Vi Mohamed1,2,3, Alexandre Desjardins1,2,3

  • 1Research Center of the University of Montreal Hospital (CRCHUM), Montréal, Québec, Canada.

Journal of Neurochemistry
|February 22, 2017
PubMed
Summary
This summary is machine-generated.

Rab7A regulates the secretion of TAU protein, a key factor in Alzheimer's disease (AD) pathology. This finding suggests that increased RAB7A in AD brains may worsen TAU spread and disease progression.

Keywords:
Alzheimer's diseaseRab7Asecretiontau protein

More Related Videos

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

Published on: October 10, 2017

9.5K
Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia
07:18

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

9.0K

Related Experiment Videos

Last Updated: Mar 7, 2026

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
09:12

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

6.8K
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
12:55

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells

Published on: October 10, 2017

9.5K
Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia
07:18

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

9.0K

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • TAU protein is implicated in Alzheimer's disease (AD) and can spread extracellularly.
  • Rab7A, a small GTPase, is involved in intracellular trafficking and is upregulated in AD.

Purpose of the Study:

  • To investigate the role of Rab7A in the secretion of TAU protein.
  • To test the hypothesis that Rab7A regulates TAU secretion.

Main Methods:

  • Utilized primary cortical neurons and HeLa cells overexpressing human TAU.
  • Assessed TAU secretion following Rab7A deletion or manipulation of its activity (dominant-negative and constitutively active forms).
  • Examined co-localization of TAU and Rab7-positive structures.

Main Results:

  • Rab7A deletion significantly decreased TAU secretion.
  • Overexpression of dominant-negative Rab7A reduced TAU secretion, while constitutively active Rab7A increased it.
  • Partial co-localization of TAU and Rab7 suggests involvement of late endosomes in secretion.

Conclusions:

  • Rab7A plays a regulatory role in TAU secretion.
  • Upregulation of RAB7A in AD may contribute to extracellular TAU accumulation and pathology propagation.