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Related Concept Videos

Kendall's Tau Test01:16

Kendall's Tau Test

Kendall's tau test, also known as the Kendall rank coefficient test, is a nonparametric method for assessing association between two variables. This test is particularly useful for identifying significant correlations when the distributions of the sample and population are unknown. Developed in 1938 by the British statistician Sir Maurice George Kendall, the tau coefficient (denoted as τ) serves as a rank correlation coefficient, with values ranging from -1 to +1.
A τ value of +1 indicates that...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Amyloid Fibrils03:03

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NF-κB-dependent Signaling Pathway02:26

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
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Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

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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Related Experiment Video

Updated: Jun 16, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

A role for FKBP52 in Tau protein function.

Béatrice Chambraud1, Elodie Sardin, Julien Giustiniani

  • 1Institut National de la Santé et de la Recherche Médicale Unité Mixte de Recherche 788, Université Paris XI, Kremlin Bicêtre 94276, France.

Proceedings of the National Academy of Sciences of the United States of America
|February 6, 2010
PubMed
Summary

FKBP52 directly binds to Tau protein, particularly its hyperphosphorylated form, impacting microtubule assembly and neurite outgrowth. This interaction suggests FKBP52

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Using Live-Cell Imaging to Measure the Effects of Pathological Proteins on Axonal Transport in Primary Hippocampal Neurons
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Using Live-Cell Imaging to Measure the Effects of Pathological Proteins on Axonal Transport in Primary Hippocampal Neurons

Published on: December 22, 2023

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Tau protein is crucial for microtubule dynamics and axonal transport in neurons.
  • Aberrant Tau assembly and hyperphosphorylation are hallmarks of neurodegenerative tauopathies like Alzheimer's disease.
  • FKBP52 is an FK506-binding protein family member found abundantly in the brain.

Purpose of the Study:

  • To investigate the biochemical and functional interactions between FKBP52 and Tau protein.
  • To determine if FKBP52 influences Tau's role in microtubule assembly and neuronal function.

Main Methods:

  • Biochemical assays to confirm direct binding between FKBP52 and Tau.
  • Immunofluorescence to assess colocalization of FKBP52 and Tau in neuronal axons.
  • Cell culture experiments (differentiated PC12 cells) to study the functional effects of FKBP52 overexpression on Tau and neurite length.

Main Results:

  • FKBP52 directly and specifically binds to Tau, with a preference for hyperphosphorylated Tau.
  • FKBP52 and Tau colocalize in the distal regions of neuronal axons.
  • FKBP52 antagonizes Tau's ability to promote microtubule assembly and reduces neurite length upon overexpression.

Conclusions:

  • FKBP52 plays a significant role in regulating Tau function.
  • The interaction between FKBP52 and Tau may be a key factor in the pathogenesis of tauopathies.
  • FKBP52 represents a potential target for modulating Tau-induced neurodegeneration.