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

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.1K
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...
13.1K
Phosphorylation01:02

Phosphorylation

50.3K
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...
50.3K

You might also read

Related Articles

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

Sort by
Same author

Proximity labeling reveals unique and shared interactomes of unmodified and pyroglutamate amyloid beta in human hippocampus in Alzheimer's disease.

bioRxiv : the preprint server for biology·2026
Same author

Large-scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation.

FEBS open bio·2026
Same author

Structure-function relationship of alpha-synuclein fibrillar polymorphs derived from distinct synucleinopathies.

Molecular systems biology·2026
Same author

Physiological α-synuclein S129 phosphorylation mediates postsynaptic and nuclear interactions in the human brain.

bioRxiv : the preprint server for biology·2025
Same author

Design, Synthesis and Evaluation of the First 2-Alkynyl(aza)indole <sup>18</sup>F Probe Targeting α-Synuclein Aggregates.

Pharmaceuticals (Basel, Switzerland)·2025
Same author

Aggregation-prone alpha-synuclein proteoforms and dysregulated molecular signatures in the vermiform appendix of synucleinopathy patients.

bioRxiv : the preprint server for biology·2025
Same journal

A human-specific genetic modifier reconfigures large-scale cortical network dynamics underlying behavioral performance.

bioRxiv : the preprint server for biology·2026
Same journal

<i>Staphylococcus aureus</i> uses a eukaryotic-like uridyltransferase to make UDP-GlcNAc for cell wall synthesis.

bioRxiv : the preprint server for biology·2026
Same journal

Dynamic redistribution of eIF4F controls cap-dependent translation initiation.

bioRxiv : the preprint server for biology·2026
Same journal

When does additional information improve accuracy of RNA secondary structure prediction?

bioRxiv : the preprint server for biology·2026
Same journal

Normative brain-state trajectories reveal deviation from healthy aging in Alzheimer's disease.

bioRxiv : the preprint server for biology·2026
Same journal

Noradrenergic infraslow rhythm during sleep is the critical link between heart-rate dynamics and memory consolidation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jun 28, 2025

Recombinant &#945;- &#946;- and &#947;-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

6.7K

Alpha-synuclein aggregates are phosphatase resistant.

S G Choi1, T Tittle1, D Garcia-Prada1

  • 1Department of Neurological Sciences, Rush University Medical Center, Chicago, IL, USA.

Biorxiv : the Preprint Server for Biology
|April 22, 2024
PubMed
Summary
This summary is machine-generated.

Phosphorylation of alpha-synuclein (αsyn) at serine 129 (PSER129) occurs in healthy brains. Calf intestinal alkaline phosphatase (CIAP) treatment distinguishes aggregated PSER129 from endogenous PSER129 in synucleinopathy research.

Keywords:
Parkinson’s disease pathogenesispost-translational modificationspostmortem intervalprotein aggregation

More Related Videos

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

17.3K
Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

7.6K

Related Experiment Videos

Last Updated: Jun 28, 2025

Recombinant &#945;- &#946;- and &#947;-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

6.7K
Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

17.3K
Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

7.6K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Alpha-synuclein (αsyn) aggregation characterizes synucleinopathies.
  • Phosphorylation at serine 129 (PSER129) is a marker for pathological αsyn, but also occurs in healthy neurons.
  • Distinguishing endogenous PSER129 from aggregated PSER129 is crucial for understanding disease mechanisms.

Approach:

  • Investigated experimental conditions affecting PSER129 detection in mammalian brains.
  • Utilized calf intestinal alkaline phosphatase (CIAP) to differentiate PSER129 pools.
  • Assessed the impact of perfusion fixation and anesthetics on PSER129 levels.

Key Points:

  • Perfusion fixation significantly impacts endogenous PSER129 detection.
  • CIAP selectively dephosphorylates endogenous PSER129 but not aggregated PSER129.
  • Aggregated PSER129 is phosphatase-resistant and associated with proteinase K-resistant αsyn.

Conclusions:

  • Alpha-synuclein aggregates are resistant to phosphatase degradation.
  • CIAP pretreatment enhances the specificity of aggregated PSER129 detection in well-preserved samples.
  • This method aids in understanding PSER129 accumulation in synucleinopathies and differentiating disease markers.