Specificity of the binding of synapsin I to Src homology 3 domains.

@article{Onofri2000SpecificityOT,
  title={Specificity of the binding of synapsin I to Src homology 3 domains.},
  author={Franco Onofri and Silvia Gioved{\`i} and H T Kao and Flavia Valtorta and L Bongiorno Borbone and Pietro De Camilli and Paul Greengard and Fabio Benfenati},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 38},
  pages={29857-67}
}
Synapsins are synaptic vesicle-associated phosphoproteins involved in synapse formation and regulation of neurotransmitter release. Recently, synapsin I has been found to bind the Src homology 3 (SH3) domains of Grb2 and c-Src. In this work we have analyzed the interactions between synapsins and an array of SH3 domains belonging to proteins involved in signal transduction, cytoskeleton assembly, or endocytosis. The binding of synapsin I was specific for a subset of SH3 domains. The highest… CONTINUE READING

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Molecular Cloning: A Laboratory Manual, 2nd Ed

  • J. Sambrook, E. F. Fritsch, T. Maniatis
  • Cold Spring Harbor Laboratory,
  • 1989

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