Rapid binding of synapsin I to F- and G-actin. A study using fluorescence resonance energy transfer

P. E. Ceccaldi, F. Benfenati, E. Chieregatti, P. Greengard, F. Valtorta

Research output: Contribution to journal › Article › peer-review

Abstract

Synapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I to actin can also be demonstrated when synaptic vesicles are present in the medium and appears to be modulated by ionic strength and synapsin I phosphorylation.

Original languageEnglish
Pages (from-to)301-305
Number of pages5
JournalFEBS Letters
Volume329
Issue number3
DOIs
Publication statusPublished - Aug 30 1993

Keywords

  • Nerve terminal
  • Protein phosphorylation
  • Synaptic vesicle

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology
  • Genetics
  • Structural Biology

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