An endocytic scaffolding protein together with Synapsin regulates synaptic vesicle clustering in the drosophila neuromuscular junction

Åsa M.E. Winther, Olga Vorontsova, Kathryn A. Rees, Tuomas Näreoja, Elena Sopova, Wei Jiao, Oleg Shupliakov

Research output

7 Citations (Scopus)

Abstract

Many endocytic proteins accumulate in the reserve pool of synaptic vesicles (SVs) in synapses and relocalize to the endocytic periactive zone during neurotransmitter release. Currently little is known about their functions outside the periactive zone. Here we show that in the Drosophila neuromuscular junction (NMJ), the endocytic scaffolding protein Dap160 colocalizes during the SV cycle and forms a functional complex with the SV-associated phosphoprotein synapsin, previously implicated in SV clustering. This direct interaction is strongly enhanced under phosphorylation-promoting conditions and is essential for proper localization of synapsin at NMJs. In a dap160 rescue mutant lacking the interaction between Dap160 and synapsin, perturbed reclustering of SVs during synaptic activity is observed. Our data indicate that in addition to the function in endocytosis, Dap160 is a component of a network of protein-protein interactions that serves for clustering of SVs in conjunction with synapsin. During the SV cycle, Dap160 interacts with synapsin dispersed from SVs and helps direct synapsin back to vesicles. The proteins function in synergy to achieve efficient clustering of SVs in the reserve pool.

Original languageEnglish
Pages (from-to)14756-14770
Number of pages15
JournalJournal of Neuroscience
Volume35
Issue number44
DOIs
Publication statusPublished - 4 Nov 2015
EventECNP Congress - Barcelona
Duration: 6 Oct 20189 Oct 2018
Conference number: 31
http://www.ecnp.eu (https://www.ecnp.eu)

Fingerprint

Synapsins
Synaptic Vesicles
Neuromuscular Junction
Drosophila
Cluster Analysis
Proteins
Phosphoproteins
Endocytosis
Synapses
Neurotransmitter Agents
Phosphorylation

Scopus subject areas

  • Neuroscience(all)

Cite this

Winther, Åsa M.E. ; Vorontsova, Olga ; Rees, Kathryn A. ; Näreoja, Tuomas ; Sopova, Elena ; Jiao, Wei ; Shupliakov, Oleg. / An endocytic scaffolding protein together with Synapsin regulates synaptic vesicle clustering in the drosophila neuromuscular junction. In: Journal of Neuroscience. 2015 ; Vol. 35, No. 44. pp. 14756-14770.
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abstract = "Many endocytic proteins accumulate in the reserve pool of synaptic vesicles (SVs) in synapses and relocalize to the endocytic periactive zone during neurotransmitter release. Currently little is known about their functions outside the periactive zone. Here we show that in the Drosophila neuromuscular junction (NMJ), the endocytic scaffolding protein Dap160 colocalizes during the SV cycle and forms a functional complex with the SV-associated phosphoprotein synapsin, previously implicated in SV clustering. This direct interaction is strongly enhanced under phosphorylation-promoting conditions and is essential for proper localization of synapsin at NMJs. In a dap160 rescue mutant lacking the interaction between Dap160 and synapsin, perturbed reclustering of SVs during synaptic activity is observed. Our data indicate that in addition to the function in endocytosis, Dap160 is a component of a network of protein-protein interactions that serves for clustering of SVs in conjunction with synapsin. During the SV cycle, Dap160 interacts with synapsin dispersed from SVs and helps direct synapsin back to vesicles. The proteins function in synergy to achieve efficient clustering of SVs in the reserve pool.",
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An endocytic scaffolding protein together with Synapsin regulates synaptic vesicle clustering in the drosophila neuromuscular junction. / Winther, Åsa M.E.; Vorontsova, Olga; Rees, Kathryn A.; Näreoja, Tuomas; Sopova, Elena; Jiao, Wei; Shupliakov, Oleg.

In: Journal of Neuroscience, Vol. 35, No. 44, 04.11.2015, p. 14756-14770.

Research output

TY - JOUR

T1 - An endocytic scaffolding protein together with Synapsin regulates synaptic vesicle clustering in the drosophila neuromuscular junction

AU - Winther, Åsa M.E.

AU - Vorontsova, Olga

AU - Rees, Kathryn A.

AU - Näreoja, Tuomas

AU - Sopova, Elena

AU - Jiao, Wei

AU - Shupliakov, Oleg

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N2 - Many endocytic proteins accumulate in the reserve pool of synaptic vesicles (SVs) in synapses and relocalize to the endocytic periactive zone during neurotransmitter release. Currently little is known about their functions outside the periactive zone. Here we show that in the Drosophila neuromuscular junction (NMJ), the endocytic scaffolding protein Dap160 colocalizes during the SV cycle and forms a functional complex with the SV-associated phosphoprotein synapsin, previously implicated in SV clustering. This direct interaction is strongly enhanced under phosphorylation-promoting conditions and is essential for proper localization of synapsin at NMJs. In a dap160 rescue mutant lacking the interaction between Dap160 and synapsin, perturbed reclustering of SVs during synaptic activity is observed. Our data indicate that in addition to the function in endocytosis, Dap160 is a component of a network of protein-protein interactions that serves for clustering of SVs in conjunction with synapsin. During the SV cycle, Dap160 interacts with synapsin dispersed from SVs and helps direct synapsin back to vesicles. The proteins function in synergy to achieve efficient clustering of SVs in the reserve pool.

AB - Many endocytic proteins accumulate in the reserve pool of synaptic vesicles (SVs) in synapses and relocalize to the endocytic periactive zone during neurotransmitter release. Currently little is known about their functions outside the periactive zone. Here we show that in the Drosophila neuromuscular junction (NMJ), the endocytic scaffolding protein Dap160 colocalizes during the SV cycle and forms a functional complex with the SV-associated phosphoprotein synapsin, previously implicated in SV clustering. This direct interaction is strongly enhanced under phosphorylation-promoting conditions and is essential for proper localization of synapsin at NMJs. In a dap160 rescue mutant lacking the interaction between Dap160 and synapsin, perturbed reclustering of SVs during synaptic activity is observed. Our data indicate that in addition to the function in endocytosis, Dap160 is a component of a network of protein-protein interactions that serves for clustering of SVs in conjunction with synapsin. During the SV cycle, Dap160 interacts with synapsin dispersed from SVs and helps direct synapsin back to vesicles. The proteins function in synergy to achieve efficient clustering of SVs in the reserve pool.

KW - Drosophila neuromuscular junction

KW - Scaffolding proteins

KW - Synapse

KW - Synapsin

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