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Related Experiment Videos

Protein tyrosine phosphorylation in synaptic vesicles.

D T Pang1, J K Wang, F Valtorta

  • 1Laboratory of Molecular and Cellular Neuroscience, Rockfeller University, New York, NY 10021.

Proceedings of the National Academy of Sciences of the United States of America
|February 1, 1988
PubMed
Summary

Synaptic vesicles exhibit high protein tyrosine phosphorylation, with synaptophysin (p38) identified as a key phosphoprotein. This phosphorylation occurs within vesicles and in intact nerve terminals.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Protein tyrosine phosphorylation plays a crucial role in cellular signaling.
  • Synaptic vesicles are essential for neurotransmission.
  • Understanding protein modifications in synaptic vesicles is key to deciphering neuronal function.

Purpose of the Study:

  • To investigate endogenous protein tyrosine phosphorylation in rat forebrain synaptic vesicles.
  • To identify and characterize phosphoproteins within synaptic vesicles.
  • To determine the location and kinetics of synaptophysin tyrosine phosphorylation.

Main Methods:

  • Purification of synaptic vesicles from rat forebrain.
  • Analysis of phosphoproteins using SDS-PAGE and Western blotting.

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  • Identification of phosphotyrosine-containing proteins.
  • Lectin chromatography for glycoprotein analysis.
  • Enzyme kinetics studies for phosphorylation rates.
  • Experiments with synaptosomes to study phosphorylation in intact terminals.

    • Main Results:

    • High levels of endogenous protein tyrosine phosphorylation were observed in synaptic vesicles.
    • Four major phosphoproteins (105, 94, 38, and 30 kDa) were identified.
    • The 38-kDa phosphoprotein was confirmed as synaptophysin (p38).
    • The 105 and 94 kDa phosphoproteins are glycoproteins.
    • Synaptophysin tyrosine phosphorylation is an intravesicular reaction, reaching maximal levels rapidly.
    • Triton X-100 inhibited endogenous substrate phosphorylation but not exogenous substrate phosphorylation.
    • Tyrosine phosphorylation of synaptophysin was also observed in intact synaptosomes.

    Conclusions:

    • Synaptic vesicles contain multiple endogenous phosphotyrosine proteins, including synaptophysin.
    • Synaptophysin tyrosine phosphorylation is an intravesicular process occurring in intact nerve terminals.
    • These findings highlight the dynamic nature of protein tyrosine phosphorylation in synaptic vesicle function.