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Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Amyloid Fibrils

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Microtubule Associated Proteins (MAPs)

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...

Mitochondria

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Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...

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Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

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Related Experiment Video

Updated: Jun 21, 2025

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

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

Published on: October 10, 2017

Cellular and pathological functions of tau.

Celeste Parra Bravo^1,2, Sarah A Naguib¹, Li Gan^3,4

¹Helen and Robert Appel Alzheimer's Disease Research Institute, Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY, USA.

Nature Reviews. Molecular Cell Biology

|July 16, 2024

Summary

Tau protein stabilizes microtubules but its aggregation causes neurodegenerative diseases like Alzheimer's. Understanding tau pathology is key to developing new treatments for these conditions.

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Last Updated: Jun 21, 2025

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

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Published on: October 10, 2017

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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

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

Published on: December 20, 2019

Area of Science:

Neuroscience
Cell Biology
Biochemistry

Background:

Tau protein is crucial for microtubule stability in neurons.
Tauopathies, including Alzheimer's disease, involve abnormal tau protein aggregation.
Factors like mutations, stress, and post-translational modifications promote tau aggregation and hinder clearance.

Purpose of the Study:

To review recent advances in understanding tau protein's cellular functions.
To explore the pathology of tau inclusions in neurodegenerative diseases.
To discuss potential therapeutic strategies targeting tau.

Main Methods:

Review of recent scientific literature.
Analysis of data from cryo-electron microscopy.
Examination of human induced pluripotent stem cell disease models.

Main Results:

Tau aggregation is strongly linked to neurodegenerative disease progression and severity.
Technological advancements have improved understanding of tau aggregate structures and toxicity mechanisms.
Insights into tau's diverse cellular roles have been elucidated.

Conclusions:

Pathological tau accumulation is a central feature of neurodegenerative diseases.
Further research into tau biology and pathology is essential for therapeutic development.
Targeting tau aggregation and propagation offers potential therapeutic avenues.