The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses

Åsa M.E. Winther, Wei Jiao, Olga Vorontsova, Kathryn A. Rees, Tong Wey Koh, Elena Sopova, Karen L. Schulze, Hugo J. Bellen, Oleg Shupliakov

Результат исследований: Научные публикации в периодических изданияхстатья

15 Цитирования (Scopus)

Выдержка

Dynamin-associated protein 160 kDa (Dap160)/intersectin interacts with several synaptic proteins and affects endocytosis and synapse development. The functional role of the different protein interaction domains is not well understood. Here we show that Drosophila Dap160 lacking the dynamin-binding SH3 domains does not affect the development of the neuromuscular junction but plays a key role in synaptic vesicle recycling. dap160 mutants lacking dynamin-interacting domains no longer accumulate dynamin properly at the periactive zone, and it becomes dispersed in the bouton during stimulation. This is accompanied by a reduction in uptake of the dye FM1-43 and an accumulation of large vesicles and membrane invaginations. However, we do not observe an increase in the number of clathrin-coated intermediates. We also note a depression in evoked excitatory junction potentials (EJPs) during high-rate stimulation, accompanied by aberrantly large miniature EJPs. The data reveal the important role of Dap160 in the targeting of dynamin to the periactive zone, where it is required to suppress bulk synaptic vesicle membrane retrieval during high-frequency activity.

Язык оригиналаанглийский
Страницы (с-по)1021-1031
Число страниц11
ЖурналJournal of Cell Science
Том126
Номер выпуска4
DOI
СостояниеОпубликовано - 15 фев 2013

Отпечаток

Dynamins
Synapses
Membranes
Proteins
Synaptic Vesicles
Protein Interaction Domains and Motifs
Synaptic Membranes
Clathrin
src Homology Domains
Neuromuscular Junction
Endocytosis
intersectin 1
Coloring Agents

Предметные области Scopus

  • Клеточная биология

Цитировать

Winther, Å. M. E., Jiao, W., Vorontsova, O., Rees, K. A., Koh, T. W., Sopova, E., ... Shupliakov, O. (2013). The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses. Journal of Cell Science, 126(4), 1021-1031. https://doi.org/10.1242/jcs.118968
Winther, Åsa M.E. ; Jiao, Wei ; Vorontsova, Olga ; Rees, Kathryn A. ; Koh, Tong Wey ; Sopova, Elena ; Schulze, Karen L. ; Bellen, Hugo J. ; Shupliakov, Oleg. / The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses. В: Journal of Cell Science. 2013 ; Том 126, № 4. стр. 1021-1031.
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abstract = "Dynamin-associated protein 160 kDa (Dap160)/intersectin interacts with several synaptic proteins and affects endocytosis and synapse development. The functional role of the different protein interaction domains is not well understood. Here we show that Drosophila Dap160 lacking the dynamin-binding SH3 domains does not affect the development of the neuromuscular junction but plays a key role in synaptic vesicle recycling. dap160 mutants lacking dynamin-interacting domains no longer accumulate dynamin properly at the periactive zone, and it becomes dispersed in the bouton during stimulation. This is accompanied by a reduction in uptake of the dye FM1-43 and an accumulation of large vesicles and membrane invaginations. However, we do not observe an increase in the number of clathrin-coated intermediates. We also note a depression in evoked excitatory junction potentials (EJPs) during high-rate stimulation, accompanied by aberrantly large miniature EJPs. The data reveal the important role of Dap160 in the targeting of dynamin to the periactive zone, where it is required to suppress bulk synaptic vesicle membrane retrieval during high-frequency activity.",
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Winther, ÅME, Jiao, W, Vorontsova, O, Rees, KA, Koh, TW, Sopova, E, Schulze, KL, Bellen, HJ & Shupliakov, O 2013, 'The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses', Journal of Cell Science, том. 126, № 4, стр. 1021-1031. https://doi.org/10.1242/jcs.118968

The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses. / Winther, Åsa M.E.; Jiao, Wei; Vorontsova, Olga; Rees, Kathryn A.; Koh, Tong Wey; Sopova, Elena; Schulze, Karen L.; Bellen, Hugo J.; Shupliakov, Oleg.

В: Journal of Cell Science, Том 126, № 4, 15.02.2013, стр. 1021-1031.

Результат исследований: Научные публикации в периодических изданияхстатья

TY - JOUR

T1 - The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses

AU - Winther, Åsa M.E.

AU - Jiao, Wei

AU - Vorontsova, Olga

AU - Rees, Kathryn A.

AU - Koh, Tong Wey

AU - Sopova, Elena

AU - Schulze, Karen L.

AU - Bellen, Hugo J.

AU - Shupliakov, Oleg

PY - 2013/2/15

Y1 - 2013/2/15

N2 - Dynamin-associated protein 160 kDa (Dap160)/intersectin interacts with several synaptic proteins and affects endocytosis and synapse development. The functional role of the different protein interaction domains is not well understood. Here we show that Drosophila Dap160 lacking the dynamin-binding SH3 domains does not affect the development of the neuromuscular junction but plays a key role in synaptic vesicle recycling. dap160 mutants lacking dynamin-interacting domains no longer accumulate dynamin properly at the periactive zone, and it becomes dispersed in the bouton during stimulation. This is accompanied by a reduction in uptake of the dye FM1-43 and an accumulation of large vesicles and membrane invaginations. However, we do not observe an increase in the number of clathrin-coated intermediates. We also note a depression in evoked excitatory junction potentials (EJPs) during high-rate stimulation, accompanied by aberrantly large miniature EJPs. The data reveal the important role of Dap160 in the targeting of dynamin to the periactive zone, where it is required to suppress bulk synaptic vesicle membrane retrieval during high-frequency activity.

AB - Dynamin-associated protein 160 kDa (Dap160)/intersectin interacts with several synaptic proteins and affects endocytosis and synapse development. The functional role of the different protein interaction domains is not well understood. Here we show that Drosophila Dap160 lacking the dynamin-binding SH3 domains does not affect the development of the neuromuscular junction but plays a key role in synaptic vesicle recycling. dap160 mutants lacking dynamin-interacting domains no longer accumulate dynamin properly at the periactive zone, and it becomes dispersed in the bouton during stimulation. This is accompanied by a reduction in uptake of the dye FM1-43 and an accumulation of large vesicles and membrane invaginations. However, we do not observe an increase in the number of clathrin-coated intermediates. We also note a depression in evoked excitatory junction potentials (EJPs) during high-rate stimulation, accompanied by aberrantly large miniature EJPs. The data reveal the important role of Dap160 in the targeting of dynamin to the periactive zone, where it is required to suppress bulk synaptic vesicle membrane retrieval during high-frequency activity.

KW - Drosophila

KW - Neuromuscular junction

KW - Protein migration

KW - Scaffolding molecules

KW - SH3 domain

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U2 - 10.1242/jcs.118968

DO - 10.1242/jcs.118968

M3 - Article

C2 - 23321638

AN - SCOPUS:84876332420

VL - 126

SP - 1021

EP - 1031

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 4

ER -

Winther ÅME, Jiao W, Vorontsova O, Rees KA, Koh TW, Sopova E и соавт. The dynamin-binding domains of Dap160/intersectin affect bulk membrane retrieval in synapses. Journal of Cell Science. 2013 Февр. 15;126(4):1021-1031. https://doi.org/10.1242/jcs.118968