Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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
UR - http://www.scopus.com/inward/record.url?scp=84876332420&partnerID=8YFLogxK
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 -
ID: 40828523