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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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Phosphorylation01:02

Phosphorylation

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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...
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Updated: Jun 24, 2025

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

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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.

Acta Neuropathologica Communications
|June 1, 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 between endogenous and aggregated PSER129 in mammalian tissues.

Keywords:
Parkinson’s disease pathogenesisPost-translational modificationsPostmortem intervalProtein aggregation

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

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

Purpose of the Study:

  • Investigate conditions for detecting and differentiating endogenous and aggregated PSER129 pools.
  • Determine the effect of fixation and anesthetic conditions on PSER129 detection.
  • Evaluate the utility of calf intestinal alkaline phosphatase (CIAP) in distinguishing PSER129 pools.

Main Methods:

  • Examined wild-type mouse brains with varying postmortem intervals.
  • Assessed the impact of anesthetics (Ketamine, xylazine) on PSER129 levels.
  • Utilized in situ CIAP treatment to assess phosphatase sensitivity of endogenous and aggregated PSER129.
  • Correlated CIAP resistance with proteinase K (PK)-resistant αsyn.

Main Results:

  • Delayed perfusion fixation significantly reduced endogenous-PSER129 detection.
  • Anesthetics did not substantially affect endogenous-PSER129 levels.
  • Endogenous-PSER129 was selectively dephosphorylated by CIAP, while aggregated forms were resistant.
  • CIAP resistance correlated with PK resistance, indicating aggregation.
  • CIAP pretreatment enabled specific detection of seeded αsyn aggregates.

Conclusions:

  • Alpha-synuclein aggregates are resistant to phosphatase treatment.
  • CIAP pretreatment enhances specificity for detecting aggregated-PSER129 in well-preserved samples.
  • This method aids in understanding PSER129 accumulation in synucleinopathies and differentiating disease-associated forms.