Get access

The behavior of α-synuclein in neurons

Authors

  • Doris L. Fortin PhD,

    1. Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA
    Search for more papers by this author
  • Venu M. Nemani PhD,

    1. Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA
    Search for more papers by this author
  • Ken Nakamura MD, PhD,

    1. Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA
    Search for more papers by this author
  • Robert H. Edwards MD

    Corresponding author
    1. Departments of Neurology and Physiology, University of California, San Francisco, San Francisco, California, USA
    • Departments of Neurology and Physiology, UCSF School of Medicine, 600 16th Street, San Francisco, CA 94158-2517
    Search for more papers by this author

  • Potential conflict of interest: None reported.

Abstract

Despite considerable evidence linking α-synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. α-Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α-synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α-synuclein, causing its dispersion from the synapse. In addition to the presumed role of α-synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society

Ancillary