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Dynamic physiological α-synuclein S129 phosphorylation is driven by neuronal activity.

Nagendran Ramalingam1, Shan-Xue Jin2, Tim E Moors2

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Phosphorylated alpha-synuclein at Serine129 (pS129) regulates neuronal activity, not just disease pathology. This discovery reveals a physiological role for pS129 in neurotransmission and brain plasticity.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Alpha-synuclein phosphorylated at Serine129 (pS129) is a key marker in synucleinopathies like Parkinson's disease.
  • The physiological function of pS129 has remained largely undefined.

Purpose of the Study:

  • To investigate the physiological role of alpha-synuclein phosphorylation at Serine129 (pS129).
  • To determine if pS129 regulates neuronal activity and neurotransmission.

Main Methods:

  • Utilized cultured neurons and mouse models to study activity-dependent alpha-synuclein phosphorylation.
  • Employed patch clamping electrophysiology and generated S129A knock-in mice.
  • Investigated the kinase/phosphatase pathways involved in pS129 regulation.

Main Results:

  • Neuronal activity robustly increases pS129 levels in a reversible, non-cytotoxic manner.
  • pS129 accumulates at presynaptic boutons and fine-tunes excitatory/inhibitory neuronal currents.
  • S129A knock-in mice exhibit impaired hippocampal plasticity, indicating a role in synaptic function.

Conclusions:

  • pS129 is a physiological regulator of neuronal activity and neurotransmission.
  • The findings provide new insights into alpha-synuclein's function beyond disease pathology.
  • pS129's role adds complexity to its interpretation as solely a synucleinopathy biomarker.