Binding of synapsin i to synaptic vesicles: Clues from the study of its interactions with liposomes

Fabio Benfenati, Flavia Valtorta, Paolo Neyroz, Paul Greengard

Research output: Contribution to journalArticlepeer-review

Abstract

Synapsin I is a major brain phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent fashion. The binding of synapsin I to synaptic vesicles involves interactions with the phospholipid and protein components of the vesicle membrane. The highly hydrophobic NH2-terminal head region of the protein binds with high-affinity to acidic phospholipids and penetrates the hydrophobic core of the membrane, whereas the basic COOH-terminal tail region does not significantly contribute to this binding. The interaction with phospholipids increases the amount of αhelix in the secondary structure of synapsin I, but does not markedly affect the microenvironment of tryptophan and cysteine residues present in the head region. The results suggest that synapsin I binds to synaptic vesicle phospholipids through amphiphilic and positively charged domains present in its NH2-terminal region and that such an interaction contributes to the high-affinity binding of synapsin I to synaptic vesicles.

Original languageEnglish
Pages (from-to)599-609
Number of pages11
JournalJournal of Liposome Research
Volume3
Issue number3
DOIs
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Pharmacology

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