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Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2.

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Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2. / Pechstein, Arndt; Bacetic, Jelena; Vahedi-Faridi, Ardeschir; Brune, Kira; Sundborger, Anna; Tomlin, Nikolay; Krainer, Georg; Vorontsova, Olga; Schäfer, Johannes G; Owe, Simen G; Cousin, Michael A; Saenger, Wolfram; Shupliakov, Oleg; Haucke, Volker.

In: P NATL ACAD SCI USA, Vol. 107, No. 9, 9, 2010, p. 4206-4211.

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

Harvard

Pechstein, A, Bacetic, J, Vahedi-Faridi, A, Brune, K, Sundborger, A, Tomlin, N, Krainer, G, Vorontsova, O, Schäfer, JG, Owe, SG, Cousin, MA, Saenger, W, Shupliakov, O & Haucke, V 2010, 'Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2.', P NATL ACAD SCI USA, vol. 107, no. 9, 9, pp. 4206-4211. <http://www.ncbi.nlm.nih.gov/pubmed/20160082?dopt=Citation>

APA

Pechstein, A., Bacetic, J., Vahedi-Faridi, A., Brune, K., Sundborger, A., Tomlin, N., Krainer, G., Vorontsova, O., Schäfer, J. G., Owe, S. G., Cousin, M. A., Saenger, W., Shupliakov, O., & Haucke, V. (2010). Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2. P NATL ACAD SCI USA, 107(9), 4206-4211. [9]. http://www.ncbi.nlm.nih.gov/pubmed/20160082?dopt=Citation

Vancouver

Pechstein A, Bacetic J, Vahedi-Faridi A, Brune K, Sundborger A, Tomlin N et al. Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2. P NATL ACAD SCI USA. 2010;107(9):4206-4211. 9.

Bibtex

@article{f0c2e2ebd5a942a3b53160cea43505c6,
title = "Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2.",
abstract = "Clathrin-mediated synaptic vesicle (SV) recycling involves the spatiotemporally controlled assembly of clathrin coat components at phosphatidylinositiol (4, 5)-bisphosphate [PI(4,5)P(2)]-enriched membrane sites within the periactive zone. Such spatiotemporal control is needed to coordinate SV cargo sorting with clathrin/AP2 recruitment and to restrain membrane fission and synaptojanin-mediated uncoating until membrane deformation and clathrin coat assembly are completed. The molecular events underlying these control mechanisms are unknown. Here we show that the endocytic SH3 domain-containing accessory protein intersectin 1 scaffolds the endocytic process by directly associating with the clathrin adaptor AP2. Acute perturbation of the intersectin 1-AP2 interaction in lamprey synapses in situ inhibits the onset of SV recycling. Structurally, complex formation can be attributed to the direct association of hydrophobic peptides within the intersectin 1 SH3A-B linker region with the {"}side sites{"} of the AP2 alpha- and beta-appendage domains. AP2 appendage association of the SH3A-B linker region inhibits binding of the inositol phosphatase synaptojanin 1 to intersectin 1. These data identify the intersectin-AP2 complex as an important regulator of clathrin-mediated SV recycling in synapses.",
keywords = "Animals, Endocytosis, Amino Acid Sequence, Molecular Sequence Data, Binding Sites, Models, Molecular, Sequence Homology, Amino Acid, Nerve Tissue Proteins/metabolism, Phosphoric Monoester Hydrolases/metabolism, src Homology Domains, Adaptor Protein Complex 2/chemistry/*metabolism, Adaptor Proteins, Vesicular Transport/chemistry/*metabolism, Lampreys, Synaptic Vesicles/*metabolism, Animals, Endocytosis, Amino Acid Sequence, Molecular Sequence Data, Binding Sites, Models, Molecular, Sequence Homology, Amino Acid, Nerve Tissue Proteins/metabolism, Phosphoric Monoester Hydrolases/metabolism, src Homology Domains, Adaptor Protein Complex 2/chemistry/*metabolism, Adaptor Proteins, Vesicular Transport/chemistry/*metabolism, Lampreys, Synaptic Vesicles/*metabolism",
author = "Arndt Pechstein and Jelena Bacetic and Ardeschir Vahedi-Faridi and Kira Brune and Anna Sundborger and Nikolay Tomlin and Georg Krainer and Olga Vorontsova and Sch{\"a}fer, {Johannes G} and Owe, {Simen G} and Cousin, {Michael A} and Wolfram Saenger and Oleg Shupliakov and Volker Haucke",
year = "2010",
language = "English",
volume = "107",
pages = "4206--4211",
journal = "P NATL ACAD SCI USA",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "9",

}

RIS

TY - JOUR

T1 - Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2.

AU - Pechstein, Arndt

AU - Bacetic, Jelena

AU - Vahedi-Faridi, Ardeschir

AU - Brune, Kira

AU - Sundborger, Anna

AU - Tomlin, Nikolay

AU - Krainer, Georg

AU - Vorontsova, Olga

AU - Schäfer, Johannes G

AU - Owe, Simen G

AU - Cousin, Michael A

AU - Saenger, Wolfram

AU - Shupliakov, Oleg

AU - Haucke, Volker

PY - 2010

Y1 - 2010

N2 - Clathrin-mediated synaptic vesicle (SV) recycling involves the spatiotemporally controlled assembly of clathrin coat components at phosphatidylinositiol (4, 5)-bisphosphate [PI(4,5)P(2)]-enriched membrane sites within the periactive zone. Such spatiotemporal control is needed to coordinate SV cargo sorting with clathrin/AP2 recruitment and to restrain membrane fission and synaptojanin-mediated uncoating until membrane deformation and clathrin coat assembly are completed. The molecular events underlying these control mechanisms are unknown. Here we show that the endocytic SH3 domain-containing accessory protein intersectin 1 scaffolds the endocytic process by directly associating with the clathrin adaptor AP2. Acute perturbation of the intersectin 1-AP2 interaction in lamprey synapses in situ inhibits the onset of SV recycling. Structurally, complex formation can be attributed to the direct association of hydrophobic peptides within the intersectin 1 SH3A-B linker region with the "side sites" of the AP2 alpha- and beta-appendage domains. AP2 appendage association of the SH3A-B linker region inhibits binding of the inositol phosphatase synaptojanin 1 to intersectin 1. These data identify the intersectin-AP2 complex as an important regulator of clathrin-mediated SV recycling in synapses.

AB - Clathrin-mediated synaptic vesicle (SV) recycling involves the spatiotemporally controlled assembly of clathrin coat components at phosphatidylinositiol (4, 5)-bisphosphate [PI(4,5)P(2)]-enriched membrane sites within the periactive zone. Such spatiotemporal control is needed to coordinate SV cargo sorting with clathrin/AP2 recruitment and to restrain membrane fission and synaptojanin-mediated uncoating until membrane deformation and clathrin coat assembly are completed. The molecular events underlying these control mechanisms are unknown. Here we show that the endocytic SH3 domain-containing accessory protein intersectin 1 scaffolds the endocytic process by directly associating with the clathrin adaptor AP2. Acute perturbation of the intersectin 1-AP2 interaction in lamprey synapses in situ inhibits the onset of SV recycling. Structurally, complex formation can be attributed to the direct association of hydrophobic peptides within the intersectin 1 SH3A-B linker region with the "side sites" of the AP2 alpha- and beta-appendage domains. AP2 appendage association of the SH3A-B linker region inhibits binding of the inositol phosphatase synaptojanin 1 to intersectin 1. These data identify the intersectin-AP2 complex as an important regulator of clathrin-mediated SV recycling in synapses.

KW - Animals

KW - Endocytosis

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Binding Sites

KW - Models, Molecular

KW - Sequence Homology, Amino Acid

KW - Nerve Tissue Proteins/metabolism

KW - Phosphoric Monoester Hydrolases/metabolism

KW - src Homology Domains

KW - Adaptor Protein Complex 2/chemistry/metabolism

KW - Adaptor Proteins, Vesicular Transport/chemistry/metabolism

KW - Lampreys

KW - Synaptic Vesicles/metabolism

KW - Animals

KW - Endocytosis

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Binding Sites

KW - Models, Molecular

KW - Sequence Homology, Amino Acid

KW - Nerve Tissue Proteins/metabolism

KW - Phosphoric Monoester Hydrolases/metabolism

KW - src Homology Domains

KW - Adaptor Protein Complex 2/chemistry/metabolism

KW - Adaptor Proteins, Vesicular Transport/chemistry/metabolism

KW - Lampreys

KW - Synaptic Vesicles/metabolism

M3 - SCORING: Journal article

VL - 107

SP - 4206

EP - 4211

JO - P NATL ACAD SCI USA

JF - P NATL ACAD SCI USA

SN - 0027-8424

IS - 9

M1 - 9

ER -