The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering (Articolo in rivista)

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  • The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1042/BJ20090762 (literal)
Alternative label
  • Ilaria MONALDI; Massimo VASSALLI; Angela BACHI; Silvia GIOVEDI'; Enrico MILLO; Flavia VALTORTA; Roberto RAITERI; Fabio BENFENATI; Anna FASSIO (2010)
    The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering
    in Biochemical journal (Lond., 1984)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ilaria MONALDI; Massimo VASSALLI; Angela BACHI; Silvia GIOVEDI'; Enrico MILLO; Flavia VALTORTA; Roberto RAITERI; Fabio BENFENATI; Anna FASSIO (literal)
Pagina inizio
  • 55 (literal)
Pagina fine
  • 64 (literal)
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  • 426 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Experimental Medicine, University of Genoa, 16132 Genoa, Italy Department of Neuroscience and Brain Technologies, The Italian Institute of Technology, 16163 Genoa, Italy CNR Institute of Biophysics, 16149 Genoa, Italy, §San Raffaele Scientific Institute, 20132 Milan, Italy, ?Istituto Nazionale di Neuroscienze, Italy, ¶Unit of Molecular Neuroscience, The Italian Institute of Technology, San Raffaele Vita-Salute University, 20132 Milan, Italy, and **Department of Biophysical Engineering and Electronics, University of Genoa, 16145 Genoa, Italy (literal)
Titolo
  • The highly conserved synapsin domain E mediates synapsin dimerization and phospholipid vesicle clustering (literal)
Abstract
  • Synapsins are abundant SV (synaptic vesicle)-associated phosphoproteins that regulate synapse formation and function. The highly conserved C-terminal domain E was shown to contribute to several synapsin functions, ranging from formation of the SV reserve pool to regulation of the kinetics of exocytosis and SV cycling, although the molecular mechanisms underlying these effects are unknown. In the present study, we used a synthetic 25-mer peptide encompassing the most conserved region of domain E (Pep-E) to analyse the role of domain E in regulating the interactions between synapsin I and liposomes mimicking the phospholipid composition of SVs (SV-liposomes) and other pre-synaptic protein partners. In affinity-chromatography and cross-linking assays, Pep-E bound to endogenous and purified exogenous synapsin I and strongly inhibited synapsin dimerization, indicating a role in synapsin oligomerization. Consistently, Pep-E (but not its scrambled version) counteracted the ability of holo-synapsin I to bind and coat phospholipid membranes, as analysed by AFM (atomic force microscopy) topographical scanning, and significantly decreased the clustering of SV-liposomes induced by holo-synapsin I in FRET (Förster resonance energy transfer) assays, suggesting a causal relationship between synapsin oligomerization and vesicle clustering. Either Pep-E or a peptide derived from domain C was necessary and sufficient to inhibit both dimerization and vesicle clustering, indicating the participation of both domains in these activities of synapsin I. The results provide a molecular explanation for the effects of domain E in nerve terminal physiology and suggest that its effects on the size and integrity of SV pools are contributed by the regulation of synapsin dimerization and SV clustering. (literal)
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