The effect of synapsin I phosphorylation upon binding of synaptic vesicles to spectrin

Aleksander F. Sikorski, Steven Goodman

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

We have previously demonstrated that brain spectrin is attached to small spherical synaptic vesicles via synapsin I. These studies utilized a novel microfiltration assay in which 125I-labelled synaptic vesicles were incubated with brain spectrin which was covalently attached to cellulosic membranes. In these studies purified dephosphosynapsin I was demonstrated to competitively inhibit the binding of the synaptic vesicles to the immobilized brain spectrin with a KI = 45 nM. In the current study we demonstrate that phosphorylation of synapsin I site 1 (0.74 mol Pi/mol synapsin I) with cAMP-dependent protein kinase and sites 2 and 3 (2.0 mol Pi/mol synapsin I) with Ca2+-calmodulin kinase II had little effect upon its interaction with brain spectrin. cAMP-dependent protein kinase phosphorylated synapsin I and Ca2+-calmodulin kinase II phosphorylated synapsin I both inhibited the binding of 125I-labelled synaptic vesicles to immobilized brain spectrin with a KI of 23 nM and 34 nM respectively. We conclude that phosphorylation of synapsin I does not down-regulate the interaction of synaptic vesicles with brain spectrin.

Original languageEnglish (US)
Pages (from-to)195-198
Number of pages4
JournalBrain Research Bulletin
Volume27
Issue number2
DOIs
StatePublished - Jan 1 1991
Externally publishedYes

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Synapsins
Spectrin
Synaptic Vesicles
Phosphorylation
Brain
Calcium-Calmodulin-Dependent Protein Kinases
Cyclic AMP-Dependent Protein Kinases
Down-Regulation
Membranes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Cite this

The effect of synapsin I phosphorylation upon binding of synaptic vesicles to spectrin. / Sikorski, Aleksander F.; Goodman, Steven.

In: Brain Research Bulletin, Vol. 27, No. 2, 01.01.1991, p. 195-198.

Research output: Contribution to journalArticle

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