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Related Concept Videos

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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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,...
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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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Related Experiment Video

Updated: Mar 12, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
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Phosphorylation induces distinct alpha-synuclein strain formation.

Meng-Rong Ma1, Zhi-Wen Hu1, Yu-Fen Zhao1

  • 1Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Tsinghua University, Beijing 100084, P. R. China.

Scientific Reports
|November 18, 2016
PubMed
Summary
This summary is machine-generated.

Phosphorylation of alpha-synuclein (α-Syn) at Ser129 creates a distinct, more toxic strain. This finding reveals a new mechanism for how different alpha-synuclein strains form in neurodegenerative diseases.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Synucleinopathies are neurodegenerative diseases linked to alpha-synuclein (α-Syn) aggregation.
  • Evidence suggests α-Syn exists in different structural strains, similar to prion diseases, potentially explaining varied clinical presentations.
  • Previous methods for generating α-Syn strains involved in vitro manipulation of conditions.

Purpose of the Study:

  • To investigate if post-translational modification, specifically phosphorylation at Ser129, can induce the formation of distinct α-Syn strains.
  • To characterize the structural, propagation, and cytotoxic properties of phosphorylated α-Syn compared to wild-type α-Syn.

Main Methods:

  • Synthesis of homogeneous alpha-synuclein phosphorylated at serine 129 (pS129 α-Syn).
  • Comparison of structural characteristics, propagation capabilities, and cytotoxicity between pS129 α-Syn and wild-type α-Syn.

Main Results:

  • Phosphorylation at Ser129 induced α-Syn to form a distinct strain with unique structures.
  • The pS129 α-Syn strain exhibited altered propagation properties and significantly higher cytotoxicity compared to wild-type α-Syn.
  • This study provides the first evidence that post-translational modification can directly lead to the formation of different α-Syn strains.

Conclusions:

  • Post-translational modification, specifically phosphorylation at Ser129, is a novel mechanism for generating distinct alpha-synuclein strains.
  • These findings offer new insights into the molecular basis of synucleinopathy diversity and pathogenesis.