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

Phosphorylation01:02

Phosphorylation

54.9K
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.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
54.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.8K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.3K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.3K
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

6.0K
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...
6.0K
Amyloid Fibrils03:03

Amyloid Fibrils

12.1K
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,...
12.1K
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

920
Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
920

You might also read

Related Articles

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

Sort by
Same author

TDP-43 subtypes shape transcriptomic signatures in Alzheimer's disease.

bioRxiv : the preprint server for biology·2026
Same author

Clinical Associations of Cerebrospinal Fluid TMEM106B in Familial and Sporadic Frontotemporal Dementia.

JAMA neurology·2026
Same author

Identification of Antibody-Cognate Antigens via a High-Throughput, Affinity Chromatography-Based, Shotgun Immunoproteomics Pipeline.

Methods in molecular biology (Clifton, N.J.)·2025
Same author

Spatial proteomics to discover aging-associated alterations in the renal tubulointerstitium.

Clinical proteomics·2025
Same author

Spatial Mass Spectrometry-Based Proteomic Analysis of Normal-Appearing Glomeruli from Young and Old Adults.

Kidney360·2025
Same author

Revisiting proliferative glomerulonephritis with monoclonal immunoglobulin deposits through immunoglobulin repertoire sequencing.

Kidney international·2025

Related Experiment Video

Updated: Feb 25, 2026

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

An acetylation-phosphorylation switch that regulates tau aggregation propensity and function.

Yari Carlomagno1, Dah-Eun Chloe Chung1,2, Mei Yue1

  • 1From the Department of Neuroscience, Mayo Clinic, Jacksonville, Florida 32224.

The Journal of Biological Chemistry
|August 2, 2017
PubMed
Summary
This summary is machine-generated.

Histone deacetylase 6 (HDAC6) modifies tau protein, a key factor in tauopathies like Alzheimer's disease. This study reveals an acetylation-phosphorylation switch that regulates tau aggregation and function, offering new therapeutic targets.

Keywords:
Alzheimer diseaseTau protein (Tau)acetylationaggregationhistone deacetylase 6 (HDAC6)neurodegenerative diseasephosphorylationtauopathy

More Related Videos

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

19.1K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.5K

Related Experiment Videos

Last Updated: Feb 25, 2026

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
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

19.1K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.5K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Aberrant tau protein accumulation defines tauopathies, including Alzheimer's disease.
  • Histone deacetylase 6 (HDAC6) is known to interact with tau protein.

Purpose of the Study:

  • To map HDAC6-responsive acetylation sites on tau protein.
  • To investigate the impact of site-specific tau acetylation on its biophysical properties.
  • To elucidate the functional consequences of an identified acetylation-phosphorylation switch in tau.

Main Methods:

  • Site-specific mapping of tau acetylation responsive to HDAC6.
  • In vitro analysis of tau biophysical properties, including aggregation and microtubule assembly.
  • Assessment of tau phosphorylation at Ser-324 in mouse models and human Alzheimer's disease patients.

Main Results:

  • Several tau acetylation sites are regulated by HDAC6.
  • Acetylation at Lys-321 inhibits tau aggregation and prevents phosphorylation at Ser-324.
  • Phosphorylation at Ser-324 impairs tau's microtubule-stabilizing function and is elevated in tauopathy models and Alzheimer's disease.

Conclusions:

  • A novel Lys-321/Ser-324 acetylation-phosphorylation switch in tau coordinately regulates its polymerization and function.
  • This switch is implicated in tau pathobiology and represents a potential therapeutic target for tauopathies.
  • Further research is warranted to explore the role of pSer-324 and therapeutic modulation of this switch in vivo.