Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. / Shupliakov, Oleg; Bloom, Ona; Gustafsson, Jenny S; Kjaerulff, Ole; Low, Peter; Tomilin, Nikolay; Pieribone, Vincent A; Greengard, Paul; Brodin, Lennart.

In: Proceedings of the National Academy of Science of the United States of America, Vol. 99, No. 22, 2002, p. 14476-81.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Shupliakov, O, Bloom, O, Gustafsson, JS, Kjaerulff, O, Low, P, Tomilin, N, Pieribone, VA, Greengard, P & Brodin, L 2002, 'Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton.', Proceedings of the National Academy of Science of the United States of America, vol. 99, no. 22, pp. 14476-81. https://doi.org/10.1073/pnas.212381799

APA

Shupliakov, O., Bloom, O., Gustafsson, J. S., Kjaerulff, O., Low, P., Tomilin, N., Pieribone, V. A., Greengard, P., & Brodin, L. (2002). Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proceedings of the National Academy of Science of the United States of America, 99(22), 14476-81. https://doi.org/10.1073/pnas.212381799

Vancouver

Shupliakov O, Bloom O, Gustafsson JS, Kjaerulff O, Low P, Tomilin N et al. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proceedings of the National Academy of Science of the United States of America. 2002;99(22):14476-81. https://doi.org/10.1073/pnas.212381799

Author

Shupliakov, Oleg ; Bloom, Ona ; Gustafsson, Jenny S ; Kjaerulff, Ole ; Low, Peter ; Tomilin, Nikolay ; Pieribone, Vincent A ; Greengard, Paul ; Brodin, Lennart. / Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. In: Proceedings of the National Academy of Science of the United States of America. 2002 ; Vol. 99, No. 22. pp. 14476-81.

Bibtex

@article{17484b40752011dd8d9f000ea68e967b,
title = "Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton.",
abstract = "Actin is an abundant component of nerve terminals that has been implicated at multiple steps of the synaptic vesicle cycle, including reversible anchoring, exocytosis, and recycling of synaptic vesicles. In the present study we used the lamprey reticulospinal synapse to examine the role of actin at the site of synaptic vesicle recycling, the endocytic zone. Compounds interfering with actin function, including phalloidin, the catalytic subunit of Clostridium botulinum C2 toxin, and N-ethylmaleimide-treated myosin S1 fragments were microinjected into the axon. In unstimulated, phalloidin-injected axons actin filaments formed a thin cytomatrix adjacent to the plasma membrane around the synaptic vesicle cluster. The filaments proliferated after stimulation and extended toward the vesicle cluster. Synaptic vesicles were tethered along the filaments. Injection of N-ethylmaleimide-treated myosin S1 fragments caused accumulation of aggregates of synaptic vesicles between the endocytic zone and the vesicle cluster, suggesting that vesicle transport was inhibited. Phalloidin, as well as C2 toxin, also caused changes in the structure of clathrin-coated pits in stimulated synapses. Our data provide evidence for a critical role of actin in recycling of synaptic vesicles, which seems to involve functions both in endocytosis and in the transport of recycled vesicles to the synaptic vesicle cluster.",
author = "Oleg Shupliakov and Ona Bloom and Gustafsson, {Jenny S} and Ole Kjaerulff and Peter Low and Nikolay Tomilin and Pieribone, {Vincent A} and Paul Greengard and Lennart Brodin",
note = "Keywords: Actins; Animals; Botulinum Toxins; Cytoskeleton; Endocytosis; Lampreys; Microfilaments; Myosin Subfragments; Presynaptic Terminals; Synaptic Vesicles",
year = "2002",
doi = "10.1073/pnas.212381799",
language = "English",
volume = "99",
pages = "14476--81",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "22",

}

RIS

TY - JOUR

T1 - Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton.

AU - Shupliakov, Oleg

AU - Bloom, Ona

AU - Gustafsson, Jenny S

AU - Kjaerulff, Ole

AU - Low, Peter

AU - Tomilin, Nikolay

AU - Pieribone, Vincent A

AU - Greengard, Paul

AU - Brodin, Lennart

N1 - Keywords: Actins; Animals; Botulinum Toxins; Cytoskeleton; Endocytosis; Lampreys; Microfilaments; Myosin Subfragments; Presynaptic Terminals; Synaptic Vesicles

PY - 2002

Y1 - 2002

N2 - Actin is an abundant component of nerve terminals that has been implicated at multiple steps of the synaptic vesicle cycle, including reversible anchoring, exocytosis, and recycling of synaptic vesicles. In the present study we used the lamprey reticulospinal synapse to examine the role of actin at the site of synaptic vesicle recycling, the endocytic zone. Compounds interfering with actin function, including phalloidin, the catalytic subunit of Clostridium botulinum C2 toxin, and N-ethylmaleimide-treated myosin S1 fragments were microinjected into the axon. In unstimulated, phalloidin-injected axons actin filaments formed a thin cytomatrix adjacent to the plasma membrane around the synaptic vesicle cluster. The filaments proliferated after stimulation and extended toward the vesicle cluster. Synaptic vesicles were tethered along the filaments. Injection of N-ethylmaleimide-treated myosin S1 fragments caused accumulation of aggregates of synaptic vesicles between the endocytic zone and the vesicle cluster, suggesting that vesicle transport was inhibited. Phalloidin, as well as C2 toxin, also caused changes in the structure of clathrin-coated pits in stimulated synapses. Our data provide evidence for a critical role of actin in recycling of synaptic vesicles, which seems to involve functions both in endocytosis and in the transport of recycled vesicles to the synaptic vesicle cluster.

AB - Actin is an abundant component of nerve terminals that has been implicated at multiple steps of the synaptic vesicle cycle, including reversible anchoring, exocytosis, and recycling of synaptic vesicles. In the present study we used the lamprey reticulospinal synapse to examine the role of actin at the site of synaptic vesicle recycling, the endocytic zone. Compounds interfering with actin function, including phalloidin, the catalytic subunit of Clostridium botulinum C2 toxin, and N-ethylmaleimide-treated myosin S1 fragments were microinjected into the axon. In unstimulated, phalloidin-injected axons actin filaments formed a thin cytomatrix adjacent to the plasma membrane around the synaptic vesicle cluster. The filaments proliferated after stimulation and extended toward the vesicle cluster. Synaptic vesicles were tethered along the filaments. Injection of N-ethylmaleimide-treated myosin S1 fragments caused accumulation of aggregates of synaptic vesicles between the endocytic zone and the vesicle cluster, suggesting that vesicle transport was inhibited. Phalloidin, as well as C2 toxin, also caused changes in the structure of clathrin-coated pits in stimulated synapses. Our data provide evidence for a critical role of actin in recycling of synaptic vesicles, which seems to involve functions both in endocytosis and in the transport of recycled vesicles to the synaptic vesicle cluster.

U2 - 10.1073/pnas.212381799

DO - 10.1073/pnas.212381799

M3 - Journal article

C2 - 12381791

VL - 99

SP - 14476

EP - 14481

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 22

ER -

ID: 5749990