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Src interacts with dynamin and synapsin in neuronal cells

A Foster-Barber1, J M Bishop

  • 1G. W. Hooper Foundation, University of California, San Francisco, CA 94143-0552, USA.

Proceedings of the National Academy of Sciences of the United States of America
|May 16, 1998
PubMed
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The nonreceptor tyrosine kinase Src interacts with key proteins involved in membrane traffic, including dynamin and synapsins. This interaction suggests Src plays a role in regulating synaptic vesicle function and broader membrane transport processes.

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • Nonreceptor tyrosine kinase Src is abundant in secretory cells like neurons.
  • Src localizes to secretory vesicles and exocytosis sites.

Purpose of the Study:

  • Investigate the role of Src in regulating membrane traffic.
  • Identify neuronal proteins that interact with Src.

Main Methods:

  • Used mouse synaptosomes and PC12 cells.
  • Employed SH3 domain binding assays.
  • Performed co-precipitation and immunofluorescence studies.
  • Analyzed protein interactions via immunoprecipitation.

Main Results:

  • Src's SH3 domain bound to dynamin, synapsin Ia, and synapsin Ib.

Related Experiment Videos

  • Dynamin and synapsins co-precipitated with Src.
  • Src, dynamin, and alpha-adaptin formed a complex.
  • Src did not phosphorylate dynamin or synapsins.

    • Conclusions:

    • Src interacts with proteins regulating synaptic vesicle dynamics.
    • Src may have a general role in membrane traffic regulation.
    • Interaction directs Src kinase activity to other vesicle proteins.